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Entry: A0A1W6MW59_9RHIZ
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ID   A0A1W6MW59_9RHIZ        Unreviewed;       398 AA.
AC   A0A1W6MW59;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
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=B1812_12450 {ECO:0000313|EMBL:ARN81756.1};
OS   Methylocystis bryophila.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=655015 {ECO:0000313|EMBL:ARN81756.1, ECO:0000313|Proteomes:UP000193978};
RN   [1] {ECO:0000313|EMBL:ARN81756.1, ECO:0000313|Proteomes:UP000193978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S285 {ECO:0000313|EMBL:ARN81756.1,
RC   ECO:0000313|Proteomes:UP000193978};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate +
CC         N-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)-
CC       acetyl-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
CC       aminotransferase activity, thus carrying out the corresponding
CC       step in lysine 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; CP019948; ARN81756.1; -; Genomic_DNA.
DR   KEGG; mbry:B1812_12450; -.
DR   KO; K00821; -.
DR   BioCyc; GCF_002117405:B1812_RS12405-MONOMER; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000193978; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00707; argD; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768889};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000193978};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00768842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193978};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768841}.
FT   REGION       96     97       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   REGION      214    217       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   COILED      296    316       {ECO:0000256|SAM:Coils}.
FT   BINDING     129    129       Pyridoxal phosphate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     132    132       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     271    271       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     272    272       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01107}.
FT   MOD_RES     243    243       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
SQ   SEQUENCE   398 AA;  41990 MW;  666352DCECAE7346 CRC64;
     MTSALYPTYA RADLAFESGE GPWLVASNGG RYLDFGAGVA VNSLGHAHPR LLEALQQGAT
     RPWHVSNLYQ IPQAERLAQR LVDASFADEV FLCNSGAEAI ECAIKTARKF HAANGEPQRY
     RLITFEGAFH GRTLATLSAG GNRKYLDGFG PPVEGFDQAP FGDLAAVETL IGPETAGVLI
     ESIQGEGGIR VFPLEFLRAL RTLCDQRGLL LVVDEVQTGV GRLGSFLAIE RAGVSPDIAA
     LAKGLGGGFP IGACLATKEA AKGMTLGAHG STFGGNPLAA SIANAVLDVV LSEGFLERVK
     RLEPVLRQQL AELEDEHPQI IDSLRGEGLM FGLKTRVPNL EFLKAARDAG LLLVAAGDNV
     VRLLPPLIID ESHIAEAGKR LRAACVALES AALAGAAQ
//
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