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Database: UniProt
Entry: A0A0N9I0W7_9PSEU
LinkDB: A0A0N9I0W7_9PSEU
Original site: A0A0N9I0W7_9PSEU 
ID   A0A0N9I0W7_9PSEU        Unreviewed;       386 AA.
AC   A0A0N9I0W7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=AOZ06_15345 {ECO:0000313|EMBL:ALG08112.1};
OS   Kibdelosporangium phytohabitans.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kibdelosporangium.
OX   NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG08112.1, ECO:0000313|Proteomes:UP000063699};
RN   [1] {ECO:0000313|EMBL:ALG08112.1, ECO:0000313|Proteomes:UP000063699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG08112.1,
RC   ECO:0000313|Proteomes:UP000063699};
RA   Qin S., Xing K.;
RT   "Genome sequencing of Kibdelosporangium phytohabitans.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP012752; ALG08112.1; -; Genomic_DNA.
DR   RefSeq; WP_054290019.1; NZ_JADBEI010000002.1.
DR   AlphaFoldDB; A0A0N9I0W7; -.
DR   STRING; 860235.AOZ06_15345; -.
DR   KEGG; kphy:AOZ06_15345; -.
DR   OrthoDB; 9801052at2; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000063699; Chromosome.
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; 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:ALG08112.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000063699};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000313|EMBL:ALG08112.1}.
FT   BINDING         103..104
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         129
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         132
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         214..217
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         271
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         272
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   386 AA;  39646 MW;  238D87A99732E294 CRC64;
     MTLQQRWEAA MMNNYGTPQL GLERGAGAHV WDTDGNRYLD LLSGIAVNAL GHAHPAIVAA
     VTEQIGRLGH TSNLNINLPA LELAERLLDV AGVEGKVVFG NSGAEAVEAA LKLSRLTGRK
     KVVSTQGGFH GRTMGALTLT GQPGKRTPFE PLVPDVTHVP YGDAAALESA VDGNTAAFIV
     EPIQGEQGVV VPPEGYLQAA REITAKHGAL LILDEVQTGI GRLGTWFAFQ QVGVIPDVVT
     LAKGLGGGLP LGACLAFGDA ANLFQPGHHG TTFGGNPVCC AAGLAVLDTI ASDGLLDHVS
     AVGKEIAAGV EGLGHPLVGG VRGAGLLIGI LLREKVSAAV AAKAKDAGYL INPIQPDVIR
     LAPPLILDHD DAAQFVADLP SALEGL
//
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