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Database: UniProt
Entry: L8JNL0_9BACT
LinkDB: L8JNL0_9BACT
Original site: L8JNL0_9BACT 
ID   L8JNL0_9BACT            Unreviewed;       415 AA.
AC   L8JNL0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   25-APR-2018, entry version 34.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00645443};
DE            EC=2.8.1.7 {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00645443};
GN   ORFNames=C900_05660 {ECO:0000313|EMBL:ELR68967.1};
OS   Fulvivirga imtechensis AK7.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Fulvivirga.
OX   NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR68967.1, ECO:0000313|Proteomes:UP000011135};
RN   [1] {ECO:0000313|EMBL:ELR68967.1, ECO:0000313|Proteomes:UP000011135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK7 {ECO:0000313|EMBL:ELR68967.1,
RC   ECO:0000313|Proteomes:UP000011135};
RA   Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Fulvivirga imtechensis AK7.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium
CC       atoms from L-cysteine, L-cystine, L-selenocysteine, and L-
CC       selenocystine to produce L-alanine.
CC       {ECO:0000256|RuleBase:RU004506}.
CC   -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
CC       sulfanyl-acceptor. {ECO:0000256|RuleBase:RU004506,
CC       ECO:0000256|SAAS:SAAS00645449}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004504,
CC         ECO:0000256|SAAS:SAAS00635993};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
CC       {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00635960}.
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:ELR68967.1}.
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DR   EMBL; AMZN01000087; ELR68967.1; -; Genomic_DNA.
DR   RefSeq; WP_009582768.1; NZ_AMZN01000087.1.
DR   EnsemblBacteria; ELR68967; ELR68967; C900_05660.
DR   PATRIC; fig|1237149.3.peg.5041; -.
DR   OrthoDB; POG091H02CX; -.
DR   Proteomes; UP000011135; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000011135};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004506,
KW   ECO:0000256|SAAS:SAAS00635955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011135};
KW   Transferase {ECO:0000256|RuleBase:RU004506,
KW   ECO:0000256|SAAS:SAAS00645445}.
FT   DOMAIN       35    403       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   415 AA;  45869 MW;  BAE789DE2A90EF82 CRC64;
     MSPFSQETIK VLDIQAIREE FPILHQQVNG KPLAYFDNAA TTQKPQQVID ALDGYYKGYN
     ANIHRGIHTL AEKATKAFEE TRVALKHFLN AKEAEEIIFT KGTTEAINLV ASTYGRQNFG
     PGDEIIISGL EHHSNIVPWQ MVAEEKGAEI KVIPVKENGE LDYEHYLTLL SNKTKLVAVN
     HASNSLGTIN PIKEMISAAH KAGAKVLIDG AQASAHLEID VQALDCDFYA VSAHKFYGPT
     GTGALYGKRE LLEAMPPYQG GGEMIKDVSF EKATYNDIPY KFEAGTPNIA DVAAFKEAID
     FVDRLGKANI AAYENHLLEY ATKALSHIEH IKLVGTAQKK VSVLSFTING IHHFDIGQML
     DARGVAVRTG HHCTQPLMER YGIEGTVRAS FAVYNTEQEI DRLVEGLERI VNFMK
//
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