ID A0A3N2NGN0_9BACT Unreviewed; 405 AA.
AC A0A3N2NGN0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=EEL51_04115 {ECO:0000313|EMBL:ROT21578.1};
OS Muribaculaceae bacterium Isolate-110 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486473 {ECO:0000313|EMBL:ROT21578.1, ECO:0000313|Proteomes:UP000275373};
RN [1] {ECO:0000313|EMBL:ROT21578.1, ECO:0000313|Proteomes:UP000275373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-110 (HZI) {ECO:0000313|Proteomes:UP000275373};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT21578.1}.
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DR EMBL; RIBL01000004; ROT21578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2NGN0; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000275373; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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:SF27; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000275373}.
FT DOMAIN 23..393
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 405 AA; 44667 MW; FFD3D0A3119CE7F8 CRC64;
MDIEKIRSGF PILERKLYNR PLVYLDNTAT SQTPDTVVKA VVDGYTTTKA NVHRGVHTLS
QEATELQEAA RRRVKEWINA ASVSEVIFTR GTTEALNLVA SSFGGLMLGE GDELILTEME
HHANIVPWQL LRDRIGFTIR VVPVNAVGEL DMDAYREMFN ERTRLVSVCH ASNVLGTVNP
VKEMTAIAHG HGVPVVVDGA QAAPHIPVDV RDIDADFYAF SAHKMYGPTG VGVLYGKEKW
LEKMPPYQGG GEMIESVSFE RTTYAELPYK FEAGTPDFIG ISALAKAIDF MDETGVEQIA
AHEHELLDYT TRRMLGEIPG MRIFGQAPGK CAIISFLVGN IHHYDMGMLL DKLGVEVRTG
HHCAQPLMHV LGVEGVVRAS FAVYNTLEEC DAFIAALKRV TAILE
//
