ID ARGD_ECO57 Reviewed; 406 AA. AC Q8X4S6; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-MAY-2022, entry version 141. DE RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107}; 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}; DE EC=2.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; GN Synonyms=dapC {ECO:0000255|HAMAP-Rule:MF_01107}; GN OrderedLocusNames=Z4720, ECs4210; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic CC pathways. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N- CC acetyl-L-glutamate 5-semialdehyde; 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}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = CC (S)-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 Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01107}; 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}. 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 -!- 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 (By similarity). CC {ECO:0000250}. 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; AE005174; AAG58467.1; -; Genomic_DNA. DR EMBL; BA000007; BAB37633.1; -; Genomic_DNA. DR PIR; B91155; B91155. DR PIR; G86000; G86000. DR RefSeq; NP_312237.1; NC_002695.1. DR RefSeq; WP_000963819.1; NZ_SEKU01000003.1. DR AlphaFoldDB; Q8X4S6; -. DR SMR; Q8X4S6; -. DR STRING; 155864.EDL933_4563; -. DR EnsemblBacteria; AAG58467; AAG58467; Z4720. DR EnsemblBacteria; BAB37633; BAB37633; ECs_4210. DR GeneID; 915934; -. DR KEGG; ece:Z4720; -. DR KEGG; ecs:ECs4210; -. DR PATRIC; fig|386585.9.peg.4394; -. DR eggNOG; COG4992; Bacteria. DR HOGENOM; CLU_016922_10_1_6; -. DR OMA; MVPNYNP; -. DR UniPathway; UPA00034; UER00020. DR UniPathway; UPA00068; UER00109. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 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; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03246; arg_catab_astC; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; KW Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..406 FT /note="Acetylornithine/succinyldiaminopimelate FT aminotransferase" FT /id="PRO_0000112745" FT REGION 108..109 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT REGION 226..229 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 141 FT /note="Pyridoxal phosphate; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 144 FT /note="N2-acetyl-L-ornithine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 283 FT /note="N2-acetyl-L-ornithine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 284 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT MOD_RES 255 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" SQ SEQUENCE 406 AA; 43755 MW; 90C65E1438466979 CRC64; MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG IAVTALGHCH PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE RVVFMNSGTE ANETAFKLAR HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPSDIIH VPFNDLHAVK AVMDDHTCAV VVEPIQGEGG VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA YMHYGVTPDI LTSAKALGGG FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY KGQARDFLYA GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV AKVVGA //