ID A0A0F2PKP5_9FIRM Unreviewed; 389 AA.
AC A0A0F2PKP5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=VR67_06140 {ECO:0000313|EMBL:KJS13082.1};
OS Peptococcaceae bacterium BRH_c8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS13082.1, ECO:0000313|Proteomes:UP000033493};
RN [1] {ECO:0000313|EMBL:KJS13082.1, ECO:0000313|Proteomes:UP000033493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS13082.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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:KJS13082.1}.
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DR EMBL; LADP01000017; KJS13082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PKP5; -.
DR STRING; 1629715.VR67_06140; -.
DR PATRIC; fig|1629715.3.peg.2658; -.
DR Proteomes; UP000033493; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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; IPR010969; Cys_dSase-rel_unknwn_funct.
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; TIGR01977; am_tr_V_EF2568; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 2..366
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 389 AA; 41799 MW; 834EC5F4763EE2ED CRC64;
MIYFDNAATT WPKPPGVTDA MRCCLDDKGA NPGRSGHRMS LEAGQVVDKT RNAIARLFNI
PDRDRVIFTL NATDALNMAI KGSIKPGDHV ITTSMEHNSV TRPLYGLRRV ISVTKVPCAE
DGSLNPRKIE KAIRINTRII VITHASNVTG TVMPVREIGA LARQKGLIFI VDAAQSAGVL
DIDVQDMNID LLALPGHKGL MGPPGTGILY VGERAQVRPF REGGTGSHST DPGQPEVLPE
KYESGTLNSP GIAGLGAGLE FISQTGINTI REHELGLTRR FIESAGRMPG VKLYGPGAEA
ERAPVVSFLL EGQDTGAVGG ALDKWYNIAC RAGLHCAPDA HRTLGTLEKK LVRFSFSYFN
TASEVDFALQ CLRDIRGRDL AEITGGCSC
//
