ID F6DF17_THETG Unreviewed; 404 AA.
AC F6DF17;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Ththe16_1751 {ECO:0000313|EMBL:AEG34146.1};
OS Thermus thermophilus (strain SG0.5JP17-16).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=762633 {ECO:0000313|EMBL:AEG34146.1, ECO:0000313|Proteomes:UP000009233};
RN [1] {ECO:0000313|Proteomes:UP000009233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-16 {ECO:0000313|Proteomes:UP000009233};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA Gladden J., Woyke T.;
RT "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL Submitted (MAY-2011) 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; CP002777; AEG34146.1; -; Genomic_DNA.
DR RefSeq; WP_014510827.1; NC_017272.1.
DR AlphaFoldDB; F6DF17; -.
DR KEGG; tts:Ththe16_1751; -.
DR PATRIC; fig|762633.3.peg.1739; -.
DR HOGENOM; CLU_003433_2_5_0; -.
DR Proteomes; UP000009233; 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; 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:AEG34146.1}.
FT DOMAIN 20..389
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 404 AA; 44661 MW; 9DC184D4D8DCC948 CRC64;
MDLSTLRVDF PLIAGRPDLV YLDSAAMSQK PRRVIESLKR FYETLNANVH RGAYRLSAEA
TEAYEEARKR LARFLNANPQ EIVFVRNTTE AMNLVAYAWG LRNLKEGDEV LVTEMEHHAG
LVPWHLVAGL TGAKVKAIPL TEEGRLDLSA LDRLLTERTR VVSLVHMSNV LGTINPVAEI
AKKAKEVGAL VVVDGAQSAP HLPVDVKALG ADFFALSGHK MLGPTGAGVL WGRYEVLEGM
MPFLGGGEMI REVHVDRSTY APPPQRFEAG TPPIAEAIAL GEAACYLMEV GMEKVFAHDR
ALLEYALKRL EEVPHLRVYG PQGPDRGAVI PFTLGRLHAH DLATFLDQEG IAVRAGHHCA
QPLHRRLGLA ATARASFYLY NTKEEVDRFV EALLRIQAKY RAWL
//
