CSD_MYCTU
ID CSD_MYCTU Reviewed; 417 AA.
AC P9WQ69; L0T9P9; O53155; P63516;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; OrderedLocusNames=Rv1464; ORFNames=MTV007.11;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC produce L-alanine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44223.1; -; Genomic_DNA.
DR PIR; C70872; C70872.
DR RefSeq; NP_215980.1; NC_000962.3.
DR RefSeq; WP_003407490.1; NZ_NVQJ01000004.1.
DR AlphaFoldDB; P9WQ69; -.
DR SMR; P9WQ69; -.
DR STRING; 83332.Rv1464; -.
DR iPTMnet; P9WQ69; -.
DR PaxDb; P9WQ69; -.
DR DNASU; 886565; -.
DR GeneID; 45425442; -.
DR GeneID; 886565; -.
DR KEGG; mtu:Rv1464; -.
DR TubercuList; Rv1464; -.
DR eggNOG; COG0520; Bacteria.
DR OMA; HKLCGPT; -.
DR PhylomeDB; P9WQ69; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
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 Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..417
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150304"
FT ACT_SITE 373
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 44596 MW; 8247BE35BFF83736 CRC64;
MTASVNSLDL AAIRADFPIL KRIMRGGNPL AYLDSGATSQ RPLQVLDAER EFLTASNGAV
HRGAHQLMEE ATDAYEQGRA DIALFVGADT DELVFTKNAT EALNLVSYVL GDSRFERAVG
PGDVIVTTEL EHHANLIPWQ ELARRTGATL RWYGVTDDGR IDLDSLYLDD RVKVVAFTHH
SNVTGVLTPV SELVSRAHQS GALTVLDACQ SVPHQPVDLH ELGVDFAAFS GHKMLGPNGI
GVLYGRRELL AQMPPFLTGG SMIETVTMEG ATYAPAPQRF EAGTPMTSQV VGLAAAARYL
GAIGMAAVEA HERELVAAAI EGLSGIDGVR ILGPTSMRDR GSPVAFVVEG VHAHDVGQVL
DDGGVAVRVG HHCALPLHRR FGLAATARAS FAVYNTADEV DRLVAGVRRS RHFFGRA
