ID AL1L1_RAT Reviewed; 902 AA. AC P28037; Q5HZB2; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 3. DT 02-SEP-2026, entry version 194. DE RecName: Full=Cytosolic 10-formyltetrahydrofolate dehydrogenase {ECO:0000305|PubMed:1848231}; DE Short=10-FTHFDH {ECO:0000303|PubMed:7822273}; DE Short=FDH {ECO:0000303|PubMed:10585460}; DE EC=1.5.1.6 {ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:17884809, ECO:0000269|PubMed:1848231, ECO:0000269|PubMed:7822273}; DE AltName: Full=Aldehyde dehydrogenase family 1 member L1 {ECO:0000312|RGD:621294}; DE AltName: Full=FBP-CI; GN Name=Aldh1l1 {ECO:0000312|RGD:621294}; Synonyms=Fthfd; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=1848231; DOI=10.1016/s0021-9258(19)67743-4; RA Cook R.J., Lloyd R.S., Wagner C.; RT "Isolation and characterization of cDNA clones for rat liver 10- RT formyltetrahydrofolate dehydrogenase."; RL J. Biol. Chem. 266:4965-4973(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, RP REGION, ACTIVE SITE, SITE, AND MUTAGENESIS OF ASP-142. RX PubMed=10585460; DOI=10.1074/jbc.274.50.35777; RA Krupenko S.A., Wagner C.; RT "Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic RT centers of 10-formyltetrahydrofolate dehydrogenase."; RL J. Biol. Chem. 274:35777-35784(1999). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=3392008; DOI=10.1016/s0021-9258(19)81498-9; RA Case G.L., Kaisaki P.J., Steele R.D.; RT "Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase RT activities."; RL J. Biol. Chem. 263:10204-10207(1988). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-707. RX PubMed=7822273; DOI=10.1074/jbc.270.2.519; RA Krupenko S.A., Wagner C., Cook R.J.; RT "Cysteine 707 is involved in the dehydrogenase activity site of rat 10- RT formyltetrahydrofolate dehydrogenase."; RL J. Biol. Chem. 270:519-522(1995). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16396499; DOI=10.1021/pr0503073; RA Moser K., White F.M.; RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC- RT MS/MS."; RL J. Proteome Res. 5:98-104(2006). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHOPANTETHEINYLATION AT SER-354, DOMAIN, RP AND MUTAGENESIS OF SER-354. RX PubMed=17884809; DOI=10.1074/jbc.m707627200; RA Donato H., Krupenko N.I., Tsybovsky Y., Krupenko S.A.; RT "10-formyltetrahydrofolate dehydrogenase requires a 4'-phosphopantetheine RT prosthetic group for catalysis."; RL J. Biol. Chem. 282:34159-34166(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [9] {ECO:0007744|PDB:1S3I} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-309, AND ACTIVE SITE. RX PubMed=14729668; DOI=10.1074/jbc.m313934200; RA Chumanevich A.A., Krupenko S.A., Davies C.; RT "The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate RT dehydrogenase: mechanism of hydrolysis and its interplay with the RT dehydrogenase domain."; RL J. Biol. Chem. 279:14355-14364(2004). RN [10] {ECO:0007744|PDB:2O2P, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:2O2R} RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 397-902 IN COMPLEX WITH NADP, RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLU-673, RP ACTIVE SITE, AND REACTION MECHANISM. RX PubMed=17302434; DOI=10.1021/bi0619573; RA Tsybovsky Y., Donato H., Krupenko N.I., Davies C., Krupenko S.A.; RT "Crystal structures of the carboxyl terminal domain of rat 10- RT formyltetrahydrofolate dehydrogenase: implications for the catalytic RT mechanism of aldehyde dehydrogenases."; RL Biochemistry 46:2917-2929(2007). RN [11] {ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHM, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHP, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR} RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 397-902 IN COMPLEX WITH NADP, RP ACTIVE SITE, AND SUBUNIT. RX PubMed=21540484; DOI=10.1074/jbc.m111.221069; RA Tsybovsky Y., Krupenko S.A.; RT "Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain RT control binding and discharging of the coenzyme."; RL J. Biol. Chem. 286:23357-23367(2011). CC -!- FUNCTION: Cytosolic 10-formyltetrahydrofolate dehydrogenase that CC catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate CC to tetrahydrofolate and carbon dioxide (PubMed:10585460, CC PubMed:17302434, PubMed:17884809, PubMed:1848231, PubMed:7822273). May CC also have an NADP(+)-dependent aldehyde dehydrogenase activity towards CC formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde CC (PubMed:1848231). {ECO:0000269|PubMed:10585460, CC ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:17884809, CC ECO:0000269|PubMed:1848231, ECO:0000269|PubMed:7822273}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + NADP(+) + H2O = (6S)-5,6,7,8- CC tetrahydrofolate + CO2 + NADPH + H(+); Xref=Rhea:RHEA:10180, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:195366; EC=1.5.1.6; CC Evidence={ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434, CC ECO:0000269|PubMed:17884809, ECO:0000269|PubMed:1848231, CC ECO:0000269|PubMed:7822273}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181; CC Evidence={ECO:0000305|PubMed:1848231}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17302434, CC ECO:0000269|PubMed:21540484, ECO:0000269|PubMed:7822273}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1848231, CC ECO:0000269|PubMed:3392008}. CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:1848231}. CC -!- DOMAIN: The N-terminal hydrolase domain has an NADP-independent CC formyltetrahydrofolate hydrolase activity, releasing formate and CC tetrahydrofolate. {ECO:0000269|PubMed:10585460}. CC -!- DOMAIN: The C-terminal aldehyde dehydrogenase domain has an NADP- CC dependent dehydrogenase activity (PubMed:10585460, PubMed:17302434, CC PubMed:7822273). It catalyzes the oxidation of formate, released by the CC hydrolysis of formyltetrahydrofolate, into CO2 (Probable). CC {ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434, CC ECO:0000269|PubMed:7822273, ECO:0000305|PubMed:17884809}. CC -!- DOMAIN: The carrier domain is phosphopantetheinylated and uses the 4'- CC phosphopantetheine/4'-PP swinging arm to transfer the formyl group CC released by the N-terminal formyltetrahydrofolate hydrolase activity to CC the C-terminal aldehyde dehydrogenase domain that catalyzes its NADP- CC dependent oxidation into CO2 (PubMed:17884809). The overall NADP- CC dependent physiological reaction requires the 3 domains (N-terminal CC hydrolase, C-terminal aldehyde dehydrogenase and carrier domains) to CC convert formyltetrahydrofolate into tetrahydrofolate and CO2 CC (PubMed:10585460, PubMed:17302434, PubMed:17884809, PubMed:7822273). CC {ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434, CC ECO:0000269|PubMed:17884809, ECO:0000269|PubMed:7822273}. CC -!- PTM: Phosphopantetheinylation at Ser-354 by AASDHPPT is required for CC the formyltetrahydrofolate dehydrogenase activity. CC {ECO:0000269|PubMed:17884809}. CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family. CC {ECO:0000305|PubMed:10585460}. CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde CC dehydrogenase family. ALDH1L subfamily. {ECO:0000305|PubMed:10585460}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M59861; AAA70429.1; -; mRNA. DR EMBL; BC089101; AAH89101.1; -; mRNA. DR PIR; A23709; A60560. DR RefSeq; NP_071992.2; NM_022547.2. DR PDB; 1S3I; X-ray; 2.30 A; A=1-310. DR PDB; 2O2P; X-ray; 1.70 A; A/B/C/D=395-902. DR PDB; 2O2Q; X-ray; 2.00 A; A/B/C/D=395-902. DR PDB; 2O2R; X-ray; 2.20 A; A/B/C/D=395-902. DR PDB; 3RHJ; X-ray; 1.89 A; A/B/C/D=397-902. DR PDB; 3RHL; X-ray; 2.00 A; A/B/C/D=397-902. DR PDB; 3RHM; X-ray; 2.38 A; A/B/C/D=397-902. DR PDB; 3RHO; X-ray; 2.26 A; A/B/C/D=397-902. DR PDB; 3RHP; X-ray; 2.50 A; A/B/C/D=397-902. DR PDB; 3RHQ; X-ray; 2.10 A; A/B/C/D=397-902. DR PDB; 3RHR; X-ray; 2.30 A; A/B/C/D=397-902. DR PDB; 4GNZ; X-ray; 2.30 A; A/B/C/D=397-902. DR PDB; 4GO0; X-ray; 3.38 A; A/B/C/D=397-902. DR PDB; 4GO2; X-ray; 2.28 A; A/B/C/D=397-902. DR PDB; 7RLT; EM; 3.70 A; A/B/C/D=1-902. DR PDB; 7RLU; EM; 2.90 A; A/B/C/D=1-902. DR AlphaFoldDB; P28037; -. DR EMDB; EMD-24540; -. DR EMDB; EMD-24547; -. DR SMR; P28037; -. DR FunCoup; P28037; 129. DR STRING; 10116.ENSRNOP00000065882; -. DR ChEMBL; CHEMBL3414419; -. DR iPTMnet; P28037; -. DR PhosphoSitePlus; P28037; -. DR PaxDb; 10116-ENSRNOP00000065882; -. DR PeptideAtlas; P28037; -. DR ABCD; P28037; 3 sequenced antibodies. DR Ensembl; ENSRNOT00000075042.4; ENSRNOP00000065882.4; ENSRNOG00000047023.4. DR GeneID; 64392; -. DR KEGG; rno:64392; -. DR AGR; RGD:621294; -. DR CTD; 10840; -. DR RGD; 621294; Aldh1l1. DR eggNOG; KOG2452; Eukaryota. DR GeneTree; ENSGT00940000160913; -. DR InParanoid; P28037; -. DR BRENDA; 1.5.1.6; 5301. DR Reactome; R-RNO-196757; Metabolism of folate and pterines. DR SABIO-RK; P28037; -. DR EvolutionaryTrace; P28037; -. DR PRO; PR:P28037; -. DR Proteomes; UP000002494; Chromosome 4. DR ExpressionAtlas; P28037; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:RGD. DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IDA:UniProtKB. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:RGD. DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IDA:UniProtKB. DR GO; GO:0006081; P:aldehyde metabolic process; IBA:GO_Central. DR GO; GO:0046655; P:folic acid metabolic process; IDA:UniProtKB. DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; TAS:RGD. DR GO; GO:0035999; P:tetrahydrofolate interconversion; ISO:RGD. DR CDD; cd07140; ALDH_F1L_FTFDH; 1. DR CDD; cd08703; FDH_Hydrolase_C; 1. DR CDD; cd08647; FMT_core_FDH_N; 1. DR FunFam; 1.10.1200.10:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 1. DR FunFam; 3.10.25.10:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 1. DR FunFam; 3.40.50.170:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 1. DR FunFam; 3.40.605.10:FF:000026; Aldehyde dehydrogenase, putative; 1. DR FunFam; 3.40.309.10:FF:000008; Cytosolic 10-formyltetrahydrofolate dehydrogenase; 1. DR FunFam; 3.40.605.10:FF:000009; Cytosolic 10-formyltetrahydrofolate dehydrogenase; 1. DR Gene3D; 1.10.1200.10; ACP-like; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1. DR Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1. DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1. DR InterPro; IPR011407; 10_FTHF_DH. DR InterPro; IPR036736; ACP-like_sf. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR037022; Formyl_trans_C_sf. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR011034; Formyl_transferase-like_C_sf. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR009081; PP-bd_ACP. DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR PIRSF; PIRSF036489; 10-FTHFDH; 1. DR SUPFAM; SSF47336; ACP-like; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS00373; GART; 1. DR PDBsum; 1S3I; -. DR PDBsum; 2O2P; -. DR PDBsum; 2O2Q; -. DR PDBsum; 2O2R; -. DR PDBsum; 3RHJ; -. DR PDBsum; 3RHL; -. DR PDBsum; 3RHM; -. DR PDBsum; 3RHO; -. DR PDBsum; 3RHP; -. DR PDBsum; 3RHQ; -. DR PDBsum; 3RHR; -. DR PDBsum; 4GNZ; -. DR PDBsum; 4GO0; -. DR PDBsum; 4GO2; -. DR PDBsum; 7RLT; -. DR PDBsum; 7RLU; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; NADP; KW One-carbon metabolism; Oxidoreductase; Phosphopantetheine; Phosphoprotein; KW Reference proteome. FT CHAIN 1..902 FT /note="Cytosolic 10-formyltetrahydrofolate dehydrogenase" FT /id="PRO_0000199422" FT DOMAIN 318..395 FT /note="Carrier" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" FT REGION 1..310 FT /note="Hydrolase domain" FT /evidence="ECO:0000305|PubMed:10585460" FT REGION 417..902 FT /note="Aldehyde dehydrogenase domain" FT /evidence="ECO:0000305|PubMed:10585460" FT ACT_SITE 106 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:10585460, FT ECO:0000305|PubMed:14729668" FT ACT_SITE 673 FT /note="Proton acceptor" FT /evidence="ECO:0000305|PubMed:17302434" FT ACT_SITE 707 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:17302434, FT ECO:0000305|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:3RHO" FT BINDING 88..90 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250|UniProtKB:O75891" FT BINDING 142 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250|UniProtKB:O75891" FT BINDING 571..573 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17302434, FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR" FT BINDING 597..600 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17302434, FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR" FT BINDING 630..635 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17302434, FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR" FT BINDING 650..651 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17302434, FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR" FT BINDING 673..674 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17302434, FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, FT ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, FT ECO:0007744|PDB:3RHR" FT BINDING 757 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:21540484, FT ECO:0007744|PDB:3RHO" FT BINDING 804..806 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17302434, FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, FT ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, FT ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, FT ECO:0007744|PDB:3RHR" FT SITE 142 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000269|PubMed:10585460" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75891" FT MOD_RES 38 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8R0Y6" FT MOD_RES 354 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258, FT ECO:0000269|PubMed:17884809" FT MOD_RES 629 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75891" FT MOD_RES 631 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75891" FT MOD_RES 660 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K009" FT MOD_RES 767 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8R0Y6" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75891" FT MOD_RES 882 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3SY69" FT MUTAGEN 142 FT /note="D->A: Loss of formyltetrahydrofolate dehydrogenase FT activity. Loss of formyltetrahydrofolate hydrolase FT activity. No effect on aldehyde dehydrogenase activity." FT /evidence="ECO:0000269|PubMed:10585460" FT MUTAGEN 354 FT /note="S->A: Loss of phosphopantetheinylation. Loss of FT formyltetrahydrofolate dehydrogenase activity. No effect on FT hydrolase and aldehyde dehydrogenase activities in vitro." FT /evidence="ECO:0000269|PubMed:17884809" FT MUTAGEN 673 FT /note="E->A: Loss of aldehyde dehydrogenase activity." FT /evidence="ECO:0000269|PubMed:17302434" FT MUTAGEN 707 FT /note="C->A: Loss of formyltetrahydrofolate dehydrogenase FT activity. No effect on formyltetrahydrofolate hydrolase FT activity. No effect on NADP binding. No effect on FT homotetramerization." FT /evidence="ECO:0000269|PubMed:7822273" FT CONFLICT 51..52 FT /note="VP -> RA (in Ref. 1; AAA70429)" FT /evidence="ECO:0000305" FT CONFLICT 283..284 FT /note="DD -> EH (in Ref. 1; AAA70429)" FT /evidence="ECO:0000305" FT CONFLICT 386 FT /note="G -> E (in Ref. 1; AAA70429)" FT /evidence="ECO:0000305" FT CONFLICT 411 FT /note="K -> R (in Ref. 1; AAA70429)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="A -> R (in Ref. 1; AAA70429)" FT /evidence="ECO:0000305" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 10..21 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 25..30 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 41..49 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 92..95 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 102..108 FT /evidence="ECO:0007829|PDB:1S3I" FT TURN 110..113 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 118..124 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 128..136 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 146..153 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 169..185 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 217..225 FT /evidence="ECO:0007829|PDB:1S3I" FT TURN 226..231 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 240..249 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 276..280 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 286..294 FT /evidence="ECO:0007829|PDB:1S3I" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:1S3I" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 318..334 FT /evidence="ECO:0007829|PDB:7RLU" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 347..351 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 354..367 FT /evidence="ECO:0007829|PDB:7RLU" FT STRAND 368..370 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 375..380 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 384..395 FT /evidence="ECO:0007829|PDB:7RLU" FT STRAND 409..413 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 416..420 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 423..426 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 434..436 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 438..442 FT /evidence="ECO:0007829|PDB:2O2P" FT TURN 444..446 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 449..454 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 458..473 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 482..498 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 500..511 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 515..517 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 518..523 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 524..536 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 542..545 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 547..549 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 555..563 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 566..570 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 573..575 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 576..589 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 604..615 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 622..625 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 630..639 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 645..650 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 652..665 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 669..673 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 678..682 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 684..686 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 688..700 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 701..704 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 710..716 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 717..731 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 752..767 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 771..774 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 780..783 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 789..793 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 796..798 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 799..801 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 807..815 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 821..827 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 830..834 FT /evidence="ECO:0007829|PDB:3RHM" FT STRAND 837..839 FT /evidence="ECO:0007829|PDB:2O2P" FT HELIX 843..852 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 855..861 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 868..870 FT /evidence="ECO:0007829|PDB:7RLU" FT HELIX 876..878 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 879..881 FT /evidence="ECO:0007829|PDB:3RHQ" FT HELIX 885..890 FT /evidence="ECO:0007829|PDB:2O2P" FT STRAND 893..901 FT /evidence="ECO:0007829|PDB:2O2P" SQ SEQUENCE 902 AA; 98874 MW; 562A8CBD73D6474A CRC64; MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG VPVFKFPRWR ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV RLIAEGTAPR CPQSEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ KLTFFNSTLN TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMM PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL VEEVKELCDG LELENEDVYM ATTFRGFIQL LVRKLRGEDD ESECVINYVE KAVNKLTLQM PYQLFIGGEF VDAEGSKTYN TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI NARDRGRLLY RLADVMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEESIH NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT RDINKALYVS DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF EY //