(data stored in SCRATCH zone)

SWISSPROT: C6AZH0_RHILS

ID   C6AZH0_RHILS            Unreviewed;       399 AA.
AC   C6AZH0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
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   OrderedLocusNames=Rleg_0185 {ECO:0000313|EMBL:ACS54496.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54496.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54496.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54496.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS54496.1; -; Genomic_DNA.
DR   RefSeq; WP_012755912.1; NC_012850.1.
DR   EnsemblBacteria; ACS54496; ACS54496; Rleg_0185.
DR   KEGG; rlg:Rleg_0185; -.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00821; -.
DR   OMA; GIATCTL; -.
DR   OrthoDB; 572533at2; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000002256; 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;
DR   PRODOM; C6AZH0.
DR   SWISS-2DPAGE; C6AZH0.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768889, ECO:0000313|EMBL:ACS54496.1};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768841, ECO:0000313|EMBL:ACS54496.1}.
FT   REGION       98     99       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   REGION      216    219       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     131    131       Pyridoxal phosphate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     134    134       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     273    273       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     274    274       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01107}.
FT   MOD_RES     245    245       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
SQ   SEQUENCE   399 AA;  42341 MW;  DAC994ED07E190AE CRC64;
     MAEAAPLYDT YSRAPLRFER GEGVWLITET GERYLDFGAG VAVTSVGHSN PHVVGALKEQ
     ADKVWHLSNI YEIPGQERLA KRLTDATFAD KVFFTNSGAE ALECAIKTAR RYQFSKGHPE
     RFHIITFEGA FHGRTLATIA AGGQEKYLEG FGPKAPGFDQ VAFGDIEAVR AAITDATAGI
     LIEPVQGEGG VRPATPEFMK ALRQLCDENG LLLILDEVQT GVGRTGKLFA HEWSGVTPDI
     MAVAKGIGGG FPLGACLATS EAASGMKAGT HGSTYGGNPL AMAVGSAVLD IILADGFLQQ
     VRDVALVFRQ GLASLKDRYP DVIEDVRGEG LLLGIKAAVP SAELLQAIRA AHLLGVPAGD
     NVIRLLPPLV VTAEEAREGL SRVERAAESI RASKVKKTA
//

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