ID ARGD_SALTY Reviewed; 405 AA. AC P40732; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 179. DE RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305}; DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107}; DE Short=DapATase {ECO:0000255|HAMAP-Rule:MF_01107}; DE Short=Succinyldiaminopimelate transferase {ECO:0000255|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:17680699}; DE EC=2.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; Synonyms=dapC, dtu; GN OrderedLocusNames=STM3468; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17. RX PubMed=2403545; DOI=10.1128/jb.172.1.397-410.1990; RA Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.; RT "Chromosomal organization and expression of Escherichia coli pabA."; RL J. Bacteriol. 172:397-410(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEXES WITH PLP, CATALYTIC RP ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND PATHWAY. RX PubMed=17680699; DOI=10.1002/prot.21567; RA Rajaram V., Ratna Prasuna P., Savithri H.S., Murthy M.R.; RT "Structure of biosynthetic N-acetylornithine aminotransferase from RT Salmonella typhimurium: studies on substrate specificity and inhibitor RT binding."; RL Proteins 70:429-441(2008). CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic CC pathways. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L- CC glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000269|PubMed:17680699}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-succinyl-(2S,6S)-2,6-diaminopimelate + 2-oxoglutarate = (S)- CC 2-succinylamino-6-oxoheptanedioate + L-glutamate; CC Xref=Rhea:RHEA:11960, ChEBI:CHEBI:15685, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58087; EC=2.6.1.17; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000269|PubMed:17680699}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000269|PubMed:17680699}; CC -!- ACTIVITY REGULATION: Inhibited by gabaculine (Gcn). CC {ECO:0000269|PubMed:17680699}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=37 uM for N-acetylornithine (at pH 9.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:17680699}; CC KM=640 uM for ornithine (at pH 9.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:17680699}; CC pH dependence: CC Optimum pH is 9.5. At pH 8.0, the activity is reduced by 50%. CC {ECO:0000269|PubMed:17680699}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- CC L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000305|PubMed:17680699}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 2/3. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000269|PubMed:17680699}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- MISCELLANEOUS: The reaction catalyzed by ACOAT is highly reversible. CC This enzyme may also transaminate ornithine. CC {ECO:0000269|PubMed:17680699}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01107}. 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; AE006468; AAL22330.1; -; Genomic_DNA. DR EMBL; M32354; AAA24265.1; -; Genomic_DNA. DR EMBL; M32355; AAA27178.1; -; Genomic_DNA. DR RefSeq; NP_462371.1; NC_003197.2. DR RefSeq; WP_000190023.1; NC_003197.2. DR PDB; 2PB0; X-ray; 1.96 A; A/B=1-405. DR PDB; 2PB2; X-ray; 1.91 A; A/B=1-405. DR PDB; 4JEV; X-ray; 1.67 A; A/B=1-405. DR PDB; 4JEW; X-ray; 1.48 A; A/B=1-405. DR PDB; 4JEX; X-ray; 1.43 A; A/B=1-405. DR PDB; 4JEY; X-ray; 1.55 A; A/B=1-405. DR PDB; 4JEZ; X-ray; 1.55 A; A/B=1-405. DR PDB; 4JF0; X-ray; 2.10 A; A/B=1-405. DR PDB; 4JF1; X-ray; 1.28 A; A/B=1-405. DR AlphaFoldDB; P40732; -. DR SMR; P40732; -. DR STRING; 99287.STM3468; -. DR PaxDb; 99287-STM3468; -. DR GeneID; 1254991; -. DR KEGG; stm:STM3468; -. DR PATRIC; fig|99287.12.peg.3665; -. DR HOGENOM; CLU_016922_10_1_6; -. DR PhylomeDB; P40732; -. DR BioCyc; SENT99287:STM3468-MONOMER; -. DR SABIO-RK; P40732; -. DR UniPathway; UPA00034; UER00020. DR UniPathway; UPA00068; UER00109. DR EvolutionaryTrace; P40732; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity; EXP:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009016; F:succinyldiaminopimelate:2-oxoglutarate transaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:L-arginine biosynthetic process; IBA:GO_Central. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 1. DR FunFam; 3.90.1150.10:FF:000009; Succinylornithine transaminase; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_01107; ArgD_aminotrans_3; 1. DR InterPro; IPR017652; Ac/SucOrn_transaminase_bac. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR050103; Class-III_PLP-dep_AT. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR03246; arg_catab_astC; 1. DR NCBIfam; TIGR00707; argD; 1. DR NCBIfam; NF002325; PRK01278.1; 1. DR NCBIfam; NF003468; PRK05093.1; 1. DR NCBIfam; NF009047; PRK12381.1; 1. DR PANTHER; PTHR11986:SF122; ACETYLORNITHINE_SUCCINYLDIAMINOPIMELATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. DR PDBsum; 2PB0; -. DR PDBsum; 2PB2; -. DR PDBsum; 4JEV; -. DR PDBsum; 4JEW; -. DR PDBsum; 4JEX; -. DR PDBsum; 4JEY; -. DR PDBsum; 4JEZ; -. DR PDBsum; 4JF0; -. DR PDBsum; 4JF1; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; KW Arginine biosynthesis; Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..405 FT /note="Acetylornithine/succinyldiaminopimelate FT aminotransferase" FT /id="PRO_0000112777" FT BINDING 108..109 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107, FT ECO:0000269|PubMed:17680699" FT BINDING 141 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107, FT ECO:0000305|PubMed:17680699" FT BINDING 144 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 226..229 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107, FT ECO:0000305|PubMed:17680699" FT BINDING 283 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 284 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107, FT ECO:0000269|PubMed:17680699" FT MOD_RES 255 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107, FT ECO:0000269|PubMed:17680699" FT CONFLICT 3 FT /note="T -> I (in Ref. 2; AAA24265/AAA27178)" FT /evidence="ECO:0000305" FT HELIX 13..16 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 61..71 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 84..96 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 100..107 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 108..126 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 146..151 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 176..182 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 187..192 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:4JF1" FT TURN 197..200 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 206..219 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:4JF1" FT TURN 228..235 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 249..253 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 270..273 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:4JEX" FT HELIX 289..302 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 305..329 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 332..338 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 341..346 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 354..363 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 369..372 FT /evidence="ECO:0007829|PDB:4JF1" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:4JF1" FT HELIX 386..405 FT /evidence="ECO:0007829|PDB:4JF1" SQ SEQUENCE 405 AA; 43670 MW; 26A69C62831E986C CRC64; MATEQTAITR ATFDEVILPV YAPADFIPVK GKGSRVWDQQ GKEYIDFAGG IAVTALGHCH PALVEALKSQ GETLWHTSNV FTNEPALRLG RKLIDATFAE RVLFMNSGTE ANETAFKLAR HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPADIIH VPFNDLHAVK AVMDDHTCAV VVEPIQGEGG VQAATPEFLK GLRDLCDEHQ ALLVFDEVQC GMGRTGDLFA YMHYGVTPDI LTSAKALGGG FPVSAMLTTQ EIASAFHVGS HGSTYGGNPL ACAVAGAAFD IINTPEVLQG IHTKRQQFVQ HLQAIDEQFD IFSDIRGMGL LIGAELKPKY KGRARDFLYA GAEAGVMVLN AGADVMRFAP SLVVEEADIH EGMQRFAQAV GKVVA //