CSD_CHLPN
ID CSD_CHLPN Reviewed; 406 AA.
AC Q9Z7L5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; OrderedLocusNames=CPn_0689, CP_0057, CpB0716;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AE001363; AAD18828.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF73623.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98896.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98645.1; -; Genomic_DNA.
DR PIR; F86576; F86576.
DR PIR; G72047; G72047.
DR RefSeq; NP_224885.1; NC_000922.1.
DR RefSeq; WP_010883327.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7L5; -.
DR SMR; Q9Z7L5; -.
DR STRING; 115711.CP_0057; -.
DR EnsemblBacteria; AAD18828; AAD18828; CPn_0689.
DR EnsemblBacteria; AAF73623; AAF73623; CP_0057.
DR GeneID; 45050740; -.
DR KEGG; cpa:CP_0057; -.
DR KEGG; cpj:yfhO_1; -.
DR KEGG; cpn:CPn_0689; -.
DR KEGG; cpt:CpB0716; -.
DR PATRIC; fig|115713.3.peg.762; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_0; -.
DR OrthoDB; 446447at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..406
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150296"
FT ACT_SITE 363
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 44601 MW; 2180F627878A0F96 CRC64;
MKNLKEDFPI FAAKAKENEP FIYLDSAATT QKPQQVIDAV ANFYTSSYAT VNRAIYSSSR
NVTEAYAAVR EKVRKWVSAA SDSEIVFTRG TTAGLNLLAI SVNDLWIPKG GVVLVSEAEH
HANVLSWEIA CRRRGSLVKK IRVHDSGLID LDDLEKLLNE GAQFVSIPHV SNVTGCVQPL
QQVAELVHRY DAYLAVDGAQ GAPHLPIDVQ LWDVDFYVFS SHKIYGPTGI GVLYGKKDLL
DQLPPVEGGG DMVAIYDHQN PEYLPAPMKF EAGTPNIAGV LGLGAALDYL DGLSAKFIYD
KEIALTTYLH KELLEIPGVE ILGPSIEEPR GALIGMTIDG AHPLDLGFLL DLRGIAVRTG
HQCAQPAMER WNVGHVLRVS LGIYNDEDDI DQFILVLQDS LDKIRR
