ID A0A1Y6CER0_9PROT Unreviewed; 409 AA.
AC A0A1Y6CER0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=SAMN05428998_11797 {ECO:0000313|EMBL:SMF48556.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF48556.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SMF48556.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SMF48556.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; FWZX01000017; SMF48556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6CER0; -.
DR STRING; 560819.SAMN05428998_11797; -.
DR Proteomes; UP000192917; 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 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; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 Lyase {ECO:0000313|EMBL:SMF48556.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000192917}.
FT DOMAIN 27..396
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 409 AA; 43551 MW; 381C5F7A1A8A9FB0 CRC64;
MDQAFPSDFD PRVARRQFPG LAEPGLHYLD NAATAQVPEA VLDALRRFEV EARGNVHGTP
HRRSLAAQAA YDAARAAVAA YLNVAPREVV FTYGATSAIN LVADSLADRL GPADRVVVSW
LEHHSNLLPW QKLARRRGVR LGALPVTAEG RLDLARLGEV VRPDTRLVAV THCSNVTGAE
TDVAAVVEAA RAVGALVLLD GAQRAPHGPL DLPGLGADLY AFSGHKTYGP TGIGVLWGRS
EVLDWLPPFM VGGQMIRSVT MDEASFADPP RRFEAGTPPI AGAVGLGAAA DWALGLDWPA
IRAHERRLTA RAIAGLRALP GVRLLGPLDL ERRGPVVSFV AEGVDSLGLC RRLDRDGFAL
RSGHHCAQPL HAVLGASSSA RASFALYNEE SEVDGLLLAV ERALVELRA
//
