ID U4KF57_9VIBR Unreviewed; 415 AA.
AC U4KF57;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN Name=sufS {ECO:0000313|EMBL:CCO61821.1};
GN ORFNames=VIBNI_B2118 {ECO:0000313|EMBL:CCO61821.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61821.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61821.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357,
CC ECO:0000256|RuleBase:RU004506};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC ECO:0000256|RuleBase:RU004506}.
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DR EMBL; FO203527; CCO61821.1; -; Genomic_DNA.
DR RefSeq; WP_022562180.1; NC_022543.1.
DR AlphaFoldDB; U4KF57; -.
DR STRING; 28173.VIBNI_B2118; -.
DR KEGG; vni:VIBNI_B2118; -.
DR PATRIC; fig|1260221.3.peg.5671; -.
DR eggNOG; COG0520; Bacteria.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000016895; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd06453; SufS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01979; sufS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:CCO61821.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 29..403
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 415 AA; 45388 MW; D671F0FC451CEC05 CRC64;
MSTEINQDTN PWRKDFPTLN QEIDGKPLVY LDSAASAQTP TSVIDRMTSF YRDEYASVHR
GVHQLSAAAT DNMEQVRDKV CTFLGADTRD EIVFTKGTTE AINLIANGYL RPLLQERGDK
PSEILISNLE HHANIVPWQM LAEQFNLTVK VWEADENGEL DIQALEPLLS ENTVLVAVAH
ISNVLGARTP IESVTQLANE RGIPVLLDGA QAVMHETVDV KSLNCDFYVF SAHKLYGPTG
IGVLYGKKSL LDAMSPWEGG GAMIDKVCLP TGTTFNQAPW KFEAGTPNIA GILGLGAAID
YVQEAGLDAI AQYENQLMDY ALTQLSTIDN IEVYGKPSHR AGVIPFNLGE HHAYDVGTFL
DRYGIAVRTG HHCAMPLISS LDQSAVCRAS IALYTTREDI DALVAGLKRI NMLLG
//
