ID A0A0M2PSX8_9BACI Unreviewed; 384 AA.
AC A0A0M2PSX8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=WQ54_03040 {ECO:0000313|EMBL:KKI93601.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI93601.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI93601.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI93601.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKI93601.1}.
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DR EMBL; LATZ01000003; KKI93601.1; -; Genomic_DNA.
DR RefSeq; WP_046511944.1; NZ_LATZ01000003.1.
DR AlphaFoldDB; A0A0M2PSX8; -.
DR PATRIC; fig|1455638.3.peg.668; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000034887; 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; 3.
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|HAMAP-Rule:MF_01107,
KW ECO:0000313|EMBL:KKI93601.1};
KW 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};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000313|EMBL:KKI93601.1}.
FT BINDING 95..96
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 122
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 125
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 206..209
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 263
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 264
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ SEQUENCE 384 AA; 41595 MW; B25A383FBA38558C CRC64;
MSYLFPTYAR WNVTVKEAKG TWITDENGTK YLDFVSGIAV CNLGHANEEI IQAVNDQLAK
YWHTSNMFHQ PIQEDVAKVL VENSDGDAVF FCNSGAEANE AAIKLARKHT GKSKIVTFLQ
SFHGRTFATM SATGQEKIQQ GFGPLLQTFT YLPYNDTSSL EGLEDDVAAI MLEVVQGEGG
VIPAQQAFID KVAETCKRIG ALLIIDEIQT GIGRTGKAFG YQHYGISPDI ITSAKGLGNG
LPVGAMVGKA SLIEAFQAGS HGSTFGGNPI AMAAAKATLA KIFNEDFLKE VNEKSDYLVN
KLNRIVGSHP LVKEIRGKGL LIGIECKEQA GAMIDQLRDH HLLVIAAGPN VIRLIPPLTV
SYEEIDKAIE IIEKAFSKQT AIAH
//
