(data stored in SCRATCH zone)

SWISSPROT: D4YXM0_SPHJU

ID   D4YXM0_SPHJU            Unreviewed;       429 AA.
AC   D4YXM0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:BAI95102.1};
DE            EC=2.6.1.62 {ECO:0000313|EMBL:BAI95102.1};
GN   Name=bioA {ECO:0000313|EMBL:BAI95102.1};
GN   OrderedLocusNames=SJA_C1-02680 {ECO:0000313|EMBL:BAI95102.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95102.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95102.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AP010803; BAI95102.1; -; Genomic_DNA.
DR   RefSeq; WP_013038903.1; NC_014006.1.
DR   ProteinModelPortal; D4YXM0; -.
DR   STRING; 452662.SJA_C1-02680; -.
DR   EnsemblBacteria; BAI95102; BAI95102; SJA_C1-02680.
DR   GeneID; 29271972; -.
DR   KEGG; sjp:SJA_C1-02680; -.
DR   eggNOG; ENOG4105C8Y; Bacteria.
DR   eggNOG; COG4992; LUCA.
DR   HOGENOM; HOG000020209; -.
DR   KO; K00833; -.
DR   OMA; NGSSCIE; -.
DR   OrthoDB; POG091H01IB; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR005815; BioA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00508; bioA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXM0.
DR   SWISS-2DPAGE; D4YXM0.
KW   Aminotransferase {ECO:0000313|EMBL:BAI95102.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000313|EMBL:BAI95102.1}.
SQ   SEQUENCE   429 AA;  45688 MW;  D89B0C480D5A05A0 CRC64;
     MTSPVWHPFF QHGLNEPIPH VERAEGALLH LAGGGTLIDC IASWWVTTHG HCHPRIVAAI
     ADQAGKLDQL IFAGYTHGPA EEVAQGLVDI APRAANRDPL AHVFFSDSGS TAVEVALKMA
     LGYWHNRALD GLSEPRHRIL VLQHSYHGDT IGAMSVGERG VYNAAWSPLL FDVGTIPFPH
     AGQEQATLDA LEAACAQKPA AFIVEPLILG AGGMLIYPAH VLREMAAICA RHDVLFIADE
     VMTGWGRTGT LFACEQAGVV PDIMAVAKGI TGGAIPLAAT LASPPIFEAH RSTDRARLFY
     HSSSYTANAI ACAAAAANLA IWREEDVLGR IAALGQGMAQ RLARLAEHPA FANPRQLGVI
     AAIDLIAPDA GYLSDLAPRL RAFAQERGLL LRPLGNTIYL MPPYCLDADQ LDRVFAVLQK
     AGDAFGASA
//

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