ID A0A1C3K1Z5_9BURK Unreviewed; 393 AA.
AC A0A1C3K1Z5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107};
DE Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107};
DE EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107};
GN Name=argD {ECO:0000256|HAMAP-Rule:MF_01107};
GN ORFNames=ODI_01862 {ECO:0000313|EMBL:SBT25438.1}, ODI_R1749
GN {ECO:0000313|EMBL:SOE48953.1};
OS Orrella dioscoreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Orrella.
OX NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT25438.1, ECO:0000313|Proteomes:UP000078558};
RN [1] {ECO:0000313|EMBL:SBT25438.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT25438.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SOE48953.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE48953.1};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_01107};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01107};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01107}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC activity, thus carrying out the corresponding step in lysine
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01107}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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; FLRC01000018; SBT25438.1; -; Genomic_DNA.
DR EMBL; LT907988; SOE48953.1; -; Genomic_DNA.
DR RefSeq; WP_067753378.1; NZ_LT907988.1.
DR AlphaFoldDB; A0A1C3K1Z5; -.
DR STRING; 1851544.ODI_01862; -.
DR KEGG; odi:ODI_R1749; -.
DR OrthoDB; 3398487at2; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000078558; Chromosome i.
DR Proteomes; UP000078558; Unassembled WGS sequence.
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: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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01107};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_01107}; Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01107}; Reference proteome {ECO:0000313|Proteomes:UP000078558};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000313|EMBL:SBT25438.1}.
FT BINDING 96..97
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 131
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 215..218
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 272
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 273
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ SEQUENCE 393 AA; 41194 MW; BC0A4525FE2D7798 CRC64;
MSSSLANIYA RLPVALSHGK GVWVWDTEGR KLLDGLAGIG VSCLGHAHPK LVGAITEQAA
KLIHTSNLYE VPEQTALGER IAAIAGMQEV LFANSGAEAN EAAIKAARYY GHKQGNEFPH
IIVMESSWHG RTLGTLAATG SEKARKGFGP LPEGFIQVPY NDLAAVAAAG DKEPRVTAVL
LEALQGEGGI RPADVAYLQG LRKLCDERGW LLMLDEVQAG IGRTGKWMAY QWAGIVPDVV
TLAKGLGGGV PIGAAAFAGR ATGVFGPGNH GTTFGGGPLV SAAALATLQA LEEEGLLENA
ATVGQYLQDS LAQALAGVQG VAEIRGRGLM IGIELDRPCG VLVRRALDAG LLINVTRDKV
VRLLPPLILS REEADYLVGQ LVPLIKQFLA EQA
//
