ID N6ULG1_9HYPH Unreviewed; 299 AA. AC N6ULG1; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 29-SEP-2021, entry version 53. DE RecName: Full=Bifunctional protein FolD {ECO:0000256|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01576}; DE EC=1.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01576}; DE EC=3.5.4.9 {ECO:0000256|HAMAP-Rule:MF_01576}; GN Name=folD {ECO:0000256|HAMAP-Rule:MF_01576, GN ECO:0000313|EMBL:ENN93249.1}; GN ORFNames=m02_02550 {ECO:0000313|EMBL:ENN93249.1}; OS Bartonella bovis m02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094492 {ECO:0000313|EMBL:ENN93249.1, ECO:0000313|Proteomes:UP000014026}; RN [1] {ECO:0000313|EMBL:ENN93249.1, ECO:0000313|Proteomes:UP000014026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=m02 {ECO:0000313|Proteomes:UP000014026}; RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393; RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C., RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.; RT "A gene transfer agent and a dynamic repertoire of secretion systems hold RT the keys to the explosive radiation of the emerging pathogen Bartonella."; RL PLoS Genet. 9:E1003393-E1003393(2013). CC -!- FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to CC 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- CC methenyltetrahydrofolate to 10-formyltetrahydrofolate. CC {ECO:0000256|HAMAP-Rule:MF_01576}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10- CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10- CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454, CC ChEBI:CHEBI:57455; EC=3.5.4.9; CC Evidence={ECO:0000256|ARBA:ARBA00001660, ECO:0000256|HAMAP- CC Rule:MF_01576}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|HAMAP-Rule:MF_01576}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576}. CC -!- SIMILARITY: Belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP-Rule:MF_01576}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01576}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ENN93249.1}. 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; AGWB01000003; ENN93249.1; -; Genomic_DNA. DR RefSeq; WP_010702073.1; NZ_KB915625.1. DR EnsemblBacteria; ENN93249; ENN93249; m02_02550. DR PATRIC; fig|1094492.3.peg.269; -. DR HOGENOM; CLU_034045_1_2_5; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000014026; Unassembled WGS sequence. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_01576}; Coiled coil {ECO:0000256|SAM:Coils}; KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP- KW Rule:MF_01576}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01576}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_01576}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01576}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01576}; KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP- KW Rule:MF_01576}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01576}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01576}. FT DOMAIN 4..120 FT /note="THF_DHG_CYH" FT /evidence="ECO:0000259|Pfam:PF00763" FT DOMAIN 123..290 FT /note="THF_DHG_CYH_C" FT /evidence="ECO:0000259|Pfam:PF02882" FT NP_BIND 168..170 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01576" FT COILED 8..28 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 193 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01576" FT BINDING 234 FT /note="NADP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01576" SQ SEQUENCE 299 AA; 32266 MW; 4476096F7DA20608 CRC64; MDNIIDGKKL AENTINKVKK ETKKFRNDHK IQPGIAVIIV GNDPASQVYV TSKSKKAEEC GFLSIKHTIP QDTKEEELLQ LIETLNSDPK IHGILVQLPL PAHINTNKIT QAIAVQKDVD GFHYINIGKL AANIFEDTII PCTPAGVMMI IEQQCGQDLS GLDAVIVGRS NIVGKPMAAL LMAANATVTI AHSRTRDLDE VCRSADILVV AVGCPHIIKK DWVKQGAIVI DVGINRIEAS EKGTNKTRLV GDVDFAEVKE KAAAITPVPG GVGPMTIAML MVNTLKAAAR AHKLPIPKF //