ID ARGD_ECO57 STANDARD; PRT; 405 AA. AC Q8X4S6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Acetylornithine/succinyldiaminopimelate aminotransferase (EC 2.6.1.11) DE (EC 2.6.1.17) (ACOAT) (Succinyldiaminopimelate transferase) DE (DapATase). GN Name=argD; Synonyms=dapC; OrderedLocusNames=z4720, ECs4210; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX MEDLINE=21074935; 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 SEQUENCE FROM N.A. RC STRAIN=O157:H7 / RIMD 0509952 / EHEC; RX MEDLINE=21156231; PubMed=11258796; 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 (By similarity). CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC -!- CATALYTIC ACTIVITY: N-succinyl-L-2,6-diaminoheptanedioate + 2- CC oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L- CC glutamate. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Arginine biosynthesis; fourth step. CC -!- PATHWAY: Lysine biosynthesis; diaminopimelate pathway; fourth CC step. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable). CC -!- MISCELLANEOUS: The reaction catalyzed by ACOAT is highly CC reversible. This enzyme may also transaminate ornithine (By CC similarity). CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. 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; AE005559; AAG58467.1; -. DR EMBL; AP002564; BAB37633.1; -. DR PIR; B91155; B91155. DR PIR; G86000; G86000. DR HSSP; P12995; 1QJ3. DR HAMAP; MF_01107; -; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR004636; ArgD_aminotrans. DR Pfam; PF00202; Aminotran_3; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR TIGRFAMs; TIGR01885; Orn_aminotrans; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. KW Aminotransferase; Arginine biosynthesis; Complete proteome; KW Lysine biosynthesis; Pyridoxal phosphate; Transferase. FT INIT_MET 0 0 By similarity. FT BINDING 254 254 Pyridoxal phosphate (By similarity). SQ SEQUENCE 405 AA; 43623 MW; B671B58FC77E03D6 CRC64; AIEQTAITRA TFDEVILPIY APAEFIPVKG QGSRIWDQQG KEYVDFAGGI AVTALGHCHP ALVNALKTQG ETLWHISNVF TNEPALRLGR KLIEATFAER VVFMNSGTEA NETAFKLARH YACVRHSPFK TKIIAFHNAF HGRSLFTVSV GGQPKYSDGF GPKPSDIIHV PFNDLHAVKA VMDDHTCAVV VEPIQGEGGV TAATPEFLQG LRELCDQHQA LLVFDEVQCG MGRTGDLFAY MHYGVTPDIL TSAKALGGGF PISAMLTTAE IASAFHPGSH GSTYGGNPLA CAVAGAAFDI INTPEVLEGI QAKRQRFVDH LQKIDQQYDV FSDIRGMGLL IGAELKPQYK GQARDFLYAG AEAGVMVLNA GPDVMRFAPS LVVEDADIDE GMQRFAHAVA KVVGA //