(data stored in ACNUC7421 zone)

SWISSPROT: C7QJ83_CATAD

ID   C7QJ83_CATAD            Unreviewed;       462 AA.
AC   C7QJ83;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACU69225.1};
GN   OrderedLocusNames=Caci_0272 {ECO:0000313|EMBL:ACU69225.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69225.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69225.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001700; ACU69225.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJ83; -.
DR   STRING; 479433.Caci_0272; -.
DR   EnsemblBacteria; ACU69225; ACU69225; Caci_0272.
DR   KEGG; cai:Caci_0272; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   KO; K15372; -.
DR   OMA; FRIAPPI; -.
DR   OrthoDB; POG091H03LZ; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJ83.
DR   SWISS-2DPAGE; C7QJ83.
KW   Aminotransferase {ECO:0000313|EMBL:ACU69225.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000313|EMBL:ACU69225.1}.
SQ   SEQUENCE   462 AA;  49517 MW;  EA96DEDFF0CC705A CRC64;
     MYVLVMTEIS SDDLKAAGAQ VFADDRAHVF HSWSAQGAIT PLPIAGAEGS YFWDYEGNRY
     LDFSSQLVNT NIGHQHPKVV AAIQEQAGKL CTIAPSFAND VRGEAARLIA ELAPGDLNYV
     FFTNGGAEAV ENAVRMARLH TGRTKVLSTY RSYHGSTSTA ISLTGDPRRW ANDAVGQSTG
     GAVHFFGPHL YRSHFHATTE AEECERALLH LEQTIQYEGP ATVAAIILET IVGTAGVLMP
     PAGYLAGVRA LCDKYGIVYI ADEVMAGFAR SGAWFAVDHW GVTPDLITFA KGSNSGYVPV
     GGVIISEKIR ETFKDRVYPG GLTYSGHPLA CASIVATINA MKEEGVIENA ARLGEEVFGP
     ALREIAAKHA SVGEVRGVGA FWALDLVRSK ETREMLVPYN ASGADAAPMN ELAAAMKARG
     VWPFVNFNRL HVVPPCTISE ADARKGLAAL DEALDVVDVY AN
//

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