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Database: UniProt
Entry: R5UA17_9BACE
LinkDB: R5UA17_9BACE
Original site: R5UA17_9BACE 
ID   R5UA17_9BACE            Unreviewed;       403 AA.
AC   R5UA17;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   05-DEC-2018, entry version 23.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|SAAS:SAAS00369712};
DE            EC=2.8.1.7 {ECO:0000256|SAAS:SAAS00369712};
GN   ORFNames=BN535_01089 {ECO:0000313|EMBL:CCZ74870.1};
OS   Bacteroides caccae CAG:21.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides; environmental samples.
OX   NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ74870.1, ECO:0000313|Proteomes:UP000017990};
RN   [1] {ECO:0000313|EMBL:CCZ74870.1, ECO:0000313|Proteomes:UP000017990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH +
CC         L-alanine; Xref=Rhea:RHEA:43892, ChEBI:CHEBI:29917,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428,
CC         Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739; EC=2.8.1.7;
CC         Evidence={ECO:0000256|SAAS:SAAS00369696};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00608953};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|SAAS:SAAS00549899}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCZ74870.1}.
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DR   EMBL; CBAN010000194; CCZ74870.1; -; Genomic_DNA.
DR   Proteomes; UP000017990; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000017990};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00435198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017990};
KW   Transferase {ECO:0000256|SAAS:SAAS00446885}.
FT   DOMAIN       23    392       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   403 AA;  44822 MW;  0349BA503F9FDBB0 CRC64;
     MDIQKIREDF PILSRTVYGK PLVYFDNGAT TQKPRLVVDA LVDEYYSVNA NVHRGVHYLS
     QQATELHEAS RESVRQFINA RSTSEVVFTR GTTESINLLV SSFGDEFMQE GDEVILSVME
     HHSNIVPWQL LAARKGIAIK VIPMNDKGEL LLDEYEKLFS ERTKIVSVVH VSNVLGTVNP
     VKEMIATAHA HGVPCLVDAA QSIPHMKVDV QDLDADFLVF SAHKIYGPTG VGVLYGKEEW
     LDRLPPYQGG GEMIQHVSFE KTTFNELPFK FEAGTPDYIG TTGLAKALDY VNGIGLEQIA
     AHEHELTTYA LQRLKEIPTM RIFGEAADRG AVISFLVGDI HHFDLGTLLD RLGIAVRTGH
     HCAQPLMQRL GIEGTVRASF AMYNTKSEID ILVAGIERVS KMF
//
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