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 07-SEP-2016, entry version 111. 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; Enterobacteriales; 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., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., 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., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and 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: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- CATALYTIC ACTIVITY: N-succinyl-L-2,6-diaminoheptanedioate + 2- CC oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L- CC glutamate. {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)- CC acetyl-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 CC reversible. This enzyme may also transaminate ornithine (By CC similarity). {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_LPWC01000263.1. DR ProteinModelPortal; Q8X4S6; -. DR SMR; Q8X4S6; 18-404. DR STRING; 155864.Z4720; -. DR EnsemblBacteria; AAG58467; AAG58467; Z4720. DR EnsemblBacteria; BAB37633; BAB37633; BAB37633. DR GeneID; 915934; -. DR KEGG; ece:Z4720; -. DR KEGG; ecs:ECs4210; -. DR PATRIC; 18357970; VBIEscCol44059_4152. DR eggNOG; ENOG4105C8Y; Bacteria. DR eggNOG; COG4992; LUCA. DR HOGENOM; HOG000020206; -. DR KO; K00821; -. DR OMA; LRHVECI; -. DR BioCyc; ECOL386585:GJFA-4180-MONOMER; -. DR BioCyc; ECOO157:ARGD-MONOMER; -. 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-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. 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; -; 2. 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_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 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 Complete proteome; Cytoplasm; Lysine biosynthesis; KW Pyridoxal phosphate; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 406 Acetylornithine/succinyldiaminopimelate FT aminotransferase. FT /FTId=PRO_0000112745. FT REGION 108 109 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT REGION 226 229 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 141 141 Pyridoxal phosphate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 144 144 N2-acetyl-L-ornithine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 283 283 N2-acetyl-L-ornithine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 284 284 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01107}. FT MOD_RES 255 255 N6-(pyridoxal phosphate)lysine. FT {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 //