ID A0A1I1ICR4_9LACT Unreviewed; 412 AA.
AC A0A1I1ICR4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=SAMN04488102_10559 {ECO:0000313|EMBL:SFC34077.1};
OS Alkalibacterium subtropicum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=753702 {ECO:0000313|EMBL:SFC34077.1, ECO:0000313|Proteomes:UP000199612};
RN [1] {ECO:0000313|EMBL:SFC34077.1, ECO:0000313|Proteomes:UP000199612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23664 {ECO:0000313|EMBL:SFC34077.1,
RC ECO:0000313|Proteomes:UP000199612};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOLT01000005; SFC34077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1ICR4; -.
DR STRING; 753702.SAMN04488102_10559; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000199612; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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:SF8; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 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 Lyase {ECO:0000313|EMBL:SFC34077.1}.
FT DOMAIN 25..396
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 412 AA; 45861 MW; 35F06CCF3C6AE211 CRC64;
MTIQSEKWRE DFPILHQVVN DEPLVYLDNA ATSQKPTAVL DALEAYYRTS NANVHRGVHT
LAERATTQYE NARETVRRFI NANETAEVLF TRGTTTGLNW LSQSLGEAVV EPGDEIVISY
MEHHSNIIPW QQLAKRKQAT LKYIELTEDG QLDMDDARKQ ITDKTKIVSL THVSNVLGVV
NPIREIAALV HDKGGVMVVD GAQAAPHMPV DVQALDADFY AFSGHKMLAP TGIGVLYGKR
KWLDRIEPVE FGGEMIDFVG LEDSTWKELP WKFEAGTPNM AGAIGLAKAI DYLESIGMRE
IMDHEQEIVD YVMPKLEQIE GLTIFGPKDP KDRTGVIAFN IDGVHPHDVA TAMDMEGVAV
RAGHHCAQPL MNYLSQPATA RASFYLYNTL ADADKFVEAL IATKEFFSYG LN
//