ID A0A134CFZ4_9FIRM Unreviewed; 411 AA.
AC A0A134CFZ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=HMPREF3191_01076 {ECO:0000313|EMBL:KXB91069.1};
OS Veillonellaceae bacterium DNF00626.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae.
OX NCBI_TaxID=1588754 {ECO:0000313|EMBL:KXB91069.1, ECO:0000313|Proteomes:UP000070542};
RN [1] {ECO:0000313|EMBL:KXB91069.1, ECO:0000313|Proteomes:UP000070542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00626 {ECO:0000313|EMBL:KXB91069.1,
RC ECO:0000313|Proteomes:UP000070542};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXB91069.1}.
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DR EMBL; LSDR01000063; KXB91069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A134CFZ4; -.
DR STRING; 1588754.HMPREF3191_01076; -.
DR PATRIC; fig|1588754.3.peg.1045; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000070542; 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 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; 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000070542};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 23..395
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 411 AA; 45892 MW; 1018CACE4BA061AD CRC64;
MNIELIRRDF PILETKVNEH QVVYFDNAAT TQRPLPVIQA VTDYLMHGNG NPHRGAHVFA
VHASEVYDTS KNVVKNFIGA RSAKEIIYTR NTSESLNLVA RSYGETHLKK GDKILITIGE
HHSNLVPWQR AAEKTGAVLE YIYVDKETGH FIEEDLKKID DPQVKIFAFA QVSNVLGVKF
DAKALIERAH AHGAVVVLDG AQSTPHMKIN VQDLDCDFFA FSGHKLCSVG GIGVLYGKEE
ILSEMEPFLL GGDMIDTVEE QKTVYADLPA KFEAGTQYVE GAVGLVAAIQ YISSIGFDSI
RQQEKILVTH ALEKLKELPF IHIVGSKNPD EKEGLISFTV EDVHPHDVAQ ILSEDGICIR
TGHHCAEPLH RYLGINATCR ASFYFYNTVD EVDYFIERLK HVRQVMGYTA S
//
