(data stored in ACNUC7421 zone)

SWISSPROT: C6B2M1_RHILS

ID   C6B2M1_RHILS            Unreviewed;       284 AA.
AC   C6B2M1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Aminotransferase class IV {ECO:0000313|EMBL:ACS54841.1};
GN   OrderedLocusNames=Rleg_0536 {ECO:0000313|EMBL:ACS54841.1};
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:ACS54841.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54841.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54841.1,
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004106}.
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DR   EMBL; CP001622; ACS54841.1; -; Genomic_DNA.
DR   RefSeq; WP_012756224.1; NC_012850.1.
DR   ProteinModelPortal; C6B2M1; -.
DR   EnsemblBacteria; ACS54841; ACS54841; Rleg_0536.
DR   KEGG; rlg:Rleg_0536; -.
DR   HOGENOM; HOG000276705; -.
DR   KO; K00824; -.
DR   OMA; ITRGVQP; -.
DR   OrthoDB; POG091H02UL; -.
DR   BioCyc; RLEG395491:GHX2-537-MONOMER; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2M1.
DR   SWISS-2DPAGE; C6B2M1.
KW   Aminotransferase {ECO:0000313|EMBL:ACS54841.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Transferase {ECO:0000313|EMBL:ACS54841.1}.
SQ   SEQUENCE   284 AA;  32024 MW;  4D8F5EFC731562D0 CRC64;
     MRQVYVNGDY LPETEARISV FDRGFLFADG VYEVTLVLDR KLVDFAGHMR RLRHSLGELD
     MAFALTNEKL LDIHRELIRR NDIEEGLVYL QVTRGAADRD FLFPADATPR TVVVFTQKKS
     LVDSPLAERG LHVITVEDLR WRRCDIKTVQ LLYPSMAKME AKSRGADDAW MVRDGFVTEG
     SSNNAYMVTL EGTVVTRDLS TDILRGITRE AVLQCAQDLQ LRIEERPFTV EEVENAAEAF
     STSSSGLVSP VVRINERVVG KGTPGPMAAR LRQLYLERSR ASAI
//

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