ID C6A0M3_THESM Unreviewed; 395 AA.
AC C6A0M3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE SubName: Full=8-amino-7-oxononanoate synthase;
GN OrderedLocusNames=TSIB_0100;
OS Thermococcus sibiricus (strain MM 739 / DSM 12597).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM 739 / DSM 12597;
RX PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon
RT Thermococcus sibiricus, isolated from a siberian oil reservoir, as
RT revealed by genome analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family.
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DR EMBL; CP001463; ACS89168.1; -; Genomic_DNA.
DR RefSeq; YP_002993517.1; NC_012883.1.
DR ProteinModelPortal; C6A0M3; -.
DR STRING; 604354.TSIB_0100; -.
DR EnsemblBacteria; ACS89168; ACS89168; TSIB_0100.
DR GeneID; 8095069; -.
DR KEGG; tsi:TSIB_0100; -.
DR eggNOG; COG0156; -.
DR HOGENOM; HOG000221022; -.
DR KO; K00639; -.
DR OMA; EYNIFAQ; -.
DR ProtClustDB; PRK06939; -.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004723; BioF.
DR InterPro; IPR010962; PyrdxlP-dep_AcTrfase_put.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR00858; bioF; 1.
DR TIGRFAMs; TIGR01825; gly_Cac_T_rel; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Pyridoxal phosphate.
SQ SEQUENCE 395 AA; 43892 MW; 5CB9886D9254DACA CRC64;
MAKLDWITEE LNELKEKGLY VRIRVLQSSQ GPWVVVDGKK VLNMCSNNYL GLAAHPKIKE
AAIRAILDYG VGAGAVRTIA GTMELHVELE EKLAKFKKRE AAILFQSGYN ANLGALSALI
KKGEDGVFVS EELNHASIID GMRLSGAEKV IYKHLNMEDL KKRLEEVKDK KKKLIVTDGV
FSMDGDLAPL PEIAELAEQY DAIVYVDDAH GEGVLGDSGR GIVDHFNLHD RVDFEMGTLS
KAFGVIGGYV AGPEEAIDYL RQRGRPFLFS SALNPPDVAA AIASVEILQH SDELVKKLWD
NTNFLQKGLR DLGYDLGNTK HPITPVMLYE EKRAQEFSKR LYEEYNIFAQ AIVYPTVPLG
TARIRLEPSA AHSKEDLQYV IDAFEDLGKK TGFLK
//
