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ARGD_RHOCB
ID   ARGD_RHOCB              Reviewed;         393 AA.
AC   P30900; D5AR54;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=RCAP_rcc03135;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=1310666; DOI=10.1101/gad.6.2.268;
RA   Beckman D.L., Trawick D.R., Kranz R.G.;
RT   "Bacterial cytochromes c biogenesis.";
RL   Genes Dev. 6:268-283(1992).
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: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}.
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DR   EMBL; CP001312; ADE86859.1; -; Genomic_DNA.
DR   EMBL; X63461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S29255; S29255.
DR   RefSeq; WP_013068832.1; NC_014034.1.
DR   AlphaFoldDB; P30900; -.
DR   SMR; P30900; -.
DR   STRING; 272942.RCAP_rcc03135; -.
DR   EnsemblBacteria; ADE86859; ADE86859; RCAP_rcc03135.
DR   GeneID; 31491922; -.
DR   KEGG; rcp:RCAP_rcc03135; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_5; -.
DR   OMA; PFMVPTY; -.
DR   OrthoDB; 572533at2; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000002361; 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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; Aminotransferase; Arginine biosynthesis;
KW   Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..393
FT                   /note="Acetylornithine aminotransferase"
FT                   /id="PRO_0000112775"
FT   BINDING         96..97
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         129
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         132
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         214..217
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         271
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         272
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   393 AA;  41517 MW;  AABAC88D4ED3B0A3 CRC64;
     MIASVLPTYT RAPLAFVRGE GSWLWTADGS RYLDLGAGIA VNALGHAAPD LVATLTEQAG
     KLWHVSNLYR IPEQERLADM LVAKTFADTV FFTNSGTEAC ELAVKMVRKH FYDKGQPERT
     EILTFSGAFH GRSSAAIAAA GTEKMVKGFG PLLPGFVHLP WGDLDAVKAA VTETTAAILI
     EPIQGEGGIR PAPEGFLRAL REICDETGTL LVFDEVQCGV ARTGKLFAHE WAGVTPDVMM
     VAKGIGGGFP LGAVLATEDA ASGMIAGTHG STYGGNPLGC AIGAKMIEIV TAPGFLDEVS
     RKAGFLRQWL EGLVAAHPDI FEEVRGQGLM LGLRLKLPPG DVVKAAYAQN LLTVPAADNV
     LRLLPALTIS EDDMAEAVRR LDAAAASLET QPA
 
 
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