CSD_CHLMU
ID CSD_CHLMU Reviewed; 400 AA.
AC Q9PLP0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; OrderedLocusNames=TC_0059;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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 -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002160; AAF73526.1; -; Genomic_DNA.
DR RefSeq; WP_010229248.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PLP0; -.
DR SMR; Q9PLP0; -.
DR STRING; 243161.TC_0059; -.
DR EnsemblBacteria; AAF73526; AAF73526; TC_0059.
DR GeneID; 1245588; -.
DR KEGG; cmu:TC_0059; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_0; -.
DR OMA; HKLCGPT; -.
DR OrthoDB; 446447at2; -.
DR Proteomes; UP000000800; 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; 3.40.640.10; -; 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; IPR016454; Cysteine_dSase.
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 PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..400
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150295"
FT ACT_SITE 358
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 43584 MW; 6B0D0FE37BE1C07C CRC64;
MYNVKEDFPI FRNQKDPYIY LDSAATTHKP QCVIDAVTDY YSFSYATVNR AIYSASHDIS
SAYWRVRSKV AAWIGARYDQ EIVFTRGTTS SLNLLAIAAN DSWLAGGTVV VSEAEHHANI
LSWEIACRRS GATVKKVRVN DEGIIDLSHL EKLLKQGVQL VSLAHVSNVS GAVLPVQEVA
FLVHRYGALL AIDGAQGVGS GPLNLSGWDV DFYAFSGHKL YAPTGIGVLY GKRELLESLP
PVEGGGDMVV VYDSESSRYQ EPPLRFEAGT PHIAGVLGLG AAIDYLQALP FSVSDHLTAL
TRFLYNRLLT IPDIQIVGPQ QGTPRGCLCS IIIPGVQASD LGFLLDGKGI AVRSGHQCSQ
PAMARWDLGH VLRASLGVYN DQQDVISFVE ALEDILRSYR