ID G0ED22_PYRF1 Unreviewed; 417 AA.
AC G0ED22;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Pyrfu_0712 {ECO:0000313|EMBL:AEM38581.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38581.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM38581.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
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; CP002838; AEM38581.1; -; Genomic_DNA.
DR RefSeq; WP_014026258.1; NC_015931.1.
DR AlphaFoldDB; G0ED22; -.
DR STRING; 694429.Pyrfu_0712; -.
DR GeneID; 11139180; -.
DR KEGG; pfm:Pyrfu_0712; -.
DR eggNOG; arCOG00065; Archaea.
DR HOGENOM; CLU_003433_2_5_2; -.
DR InParanoid; G0ED22; -.
DR Proteomes; UP000001037; Chromosome.
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:SF8; CYSTEINE DESULFURASE-RELATED; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 2.
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:UP000001037}.
FT DOMAIN 29..403
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 417 AA; 46578 MW; 178AFE6977A52977 CRC64;
MRFLPGEGFL LDYESIREDF PILSKKRIVY LDNAATTQKP RQVIEAVRRF YEESNANILR
GIYELSMKAT MLYEEAHIVV AKFIGARDWR EVVFTKNSTD SINMIAYALI GRIKSGDNIV
VTEMEHHSNF LPWVRLARLT GAELRVAPID EHGRLDMEKL ESLIDEKTRV VAIVHASNVL
GVVNDVRRVA RIAHQYDALV VVDAAQSVPH MPVNVRELEA DFLVFSGHKM LGPTGIGVLW
GRLDILEELE PPVYGGGAVK SVRVESGEVK VEYAELPWKW EPGTPNIAGA VGLAEAVRYL
QGIGLEKIEA HERTLTRMLI KMLGELDVRM VGDIPAEERV GIVSFTLDGF KPLFVALRLG
RMKIAVRAGF HCAEPLHRKL GFNEGSVRAS MYLYNGPDDI EKLVDALRGI LRGEGGS
//