ID ARGD_HAEDU Reviewed; 393 AA. AC Q7VMS5; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 04-NOV-2026, entry version 131. 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=HD_0892; OS Haemophilus ducreyi (strain 35000HP / ATCC 700724). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=233412; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., RA Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. 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}; 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 -!- SEQUENCE CAUTION: CC Sequence=AAP95778.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE017143; AAP95778.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_041603433.1; NC_002940.2. DR AlphaFoldDB; Q7VMS5; -. DR SMR; Q7VMS5; -. DR STRING; 233412.HD_0892; -. DR KEGG; hdu:HD_0892; -. DR eggNOG; COG4992; Bacteria. DR HOGENOM; CLU_016922_10_1_6; -. DR OMA; AAKLWHC; -. DR OrthoDB; 9801052at2; -. DR UniPathway; UPA00068; UER00109. DR Proteomes; UP000001022; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 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; 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; TIGR00707; argD; 1. DR NCBIfam; NF002325; PRK01278.1; 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..393 FT /note="Acetylornithine aminotransferase" FT /id="PRO_0000112747" FT BINDING 105..106 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 138 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 141 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 224..227 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 281 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT BINDING 282 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" FT MOD_RES 253 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107" SQ SEQUENCE 393 AA; 42747 MW; 419D7208D4BA20DB CRC64; MTSDQIKQLD ANYIAQTYAK FDLALSHGQG CEVWDFDGNK YLDFTSGIGV NSLGWADPDW LEAVIAQLHK LSHTSNLFYT EPSARLAKHL VQVSGLKRVF FANSGAEANE GAIKVARKYS HDKYGDTRST IISLVNSFHG RTISTLAATG QKLFHQHFFP FTAGFEHLIA NDLNAFKTRI AQNDICAIIL EVVQGEGGVC SLDQAYLQAV QGLCQVQDIL LIIDEVQTGI GRTGTMFAYQ QFELKPDIVT LAKGLAGGLP IGAFLLADKV AETLAKGDHG STFGANPVSC AAANAVLTKL EPLFLTEVMR KGQKLRKALQ SLPHVKSISG LGLMIGVEFD EHINVADVVT NCLKQGVLFL TAKTKLRMLP PLIINDEQLE RGVTVLAQVL SEM //