ID ARGD_SYNY3 Reviewed; 429 AA. AC P73133; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107}; DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; GN OrderedLocusNames=slr1022; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase CC activity, thus carrying out the corresponding step in lysine CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01107}. 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; BA000022; BAA17159.1; -; Genomic_DNA. DR PIR; S75245; S75245. DR AlphaFoldDB; P73133; -. DR SMR; P73133; -. DR IntAct; P73133; 2. DR STRING; 1148.gene:10498021; -. DR PaxDb; 1148-1652236; -. DR EnsemblBacteria; BAA17159; BAA17159; BAA17159. DR KEGG; syn:slr1022; -. DR eggNOG; COG4992; Bacteria. DR InParanoid; P73133; -. DR PhylomeDB; P73133; -. DR BioCyc; MetaCyc:SGL_RS04875-MONOMER; -. DR BRENDA; 2.6.1.11; 17663. DR BRENDA; 2.6.1.19; 17663. DR UniPathway; UPA00068; UER00109. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00610; OAT_like; 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; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR00707; argD; 1. DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; KW Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..429 FT /note="Acetylornithine aminotransferase" FT /id="PRO_0000112804" FT BINDING 126..127 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 160 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 163 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 251..254 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 307 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 308 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT MOD_RES 280 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" SQ SEQUENCE 429 AA; 46567 MW; 99FAFA3ABE4AE530 CRC64; MTYSPVVESV EAQAFAVTDL SPAAEFKTAD FDTYVMNTYG RFPIAIARGQ GSTLWDTEGK SYLDFVAGIA TCTLGHAHPA LVRAVSDQIQ KLHHVSNLYY IPEQGELAKW IVEHSCADRV FFCNSGAEAN EAAIKLVRKY AHTVLDFLEQ PVILTAKASF HGRTLATITA TGQPKYQQYF DPLVPGFDYV PYNDIRSLEN KVADLDEGNS RVAAIFLEPL QGEGGVRPGD LAYFKRVREI CDQNDILLVF DEVQVGVGRT GKLWGYEHLG VEPDIFTSAK GLAGGVPIGA MMCKKFCDVF EPGNHASTFG GNPLACAAGL AVLKTIEGDR LLDNVQARGE QLRSGLAEIK NQYPTLFTEV RGWGLINGLE ISAESSLTSV EIVKAAMEQG LLLAPAGPKV LRFVPPLVVT EAEIAQAVEI LRQAIATLV //