CSD_TREPA
ID CSD_TREPA Reviewed; 404 AA.
AC O83623;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; OrderedLocusNames=TP_0614;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65590.1; -; Genomic_DNA.
DR PIR; C71303; C71303.
DR RefSeq; WP_010882060.1; NC_021490.2.
DR AlphaFoldDB; O83623; -.
DR SMR; O83623; -.
DR STRING; 243276.TPANIC_0614; -.
DR EnsemblBacteria; AAC65590; AAC65590; TP_0614.
DR GeneID; 57879137; -.
DR KEGG; tpa:TP_0614; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_12; -.
DR OMA; HKLCGPT; -.
DR OrthoDB; 446447at2; -.
DR Proteomes; UP000000811; 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; 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 3: Inferred from homology;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150320"
FT ACT_SITE 360
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 43851 MW; 9F8464B473EA38FB CRC64;
MSGPNYKADF PLLLRSPRVH YLDSAATTQR PAPVLERVMH YHTHLNGNAG RGSHELAVES
ALLIENTRKK TAQFINAAPT HDIVFTKSCT ESLNIIAHCY ALPRLRAGDE IVLAISNHHA
NIVPWQHVCR CTGATIQWLY PDAEGNLDIQ EAQKKIRACT KIVSFSAVVN ATGAVNPAQE
LTALAHQVGA VVVIDGAQAM VHGVPNVADL GCDFFVFSGH KMFSLFGVGV LCAPHTLLES
MPPFLYGGGM VDFVTEQESV FKGAPHKYEG GSANTAAVVS LCAAIEYCES LESSAVRASV
HALDAALLAR LEELPFLETY HARARERLGI IAFNVKNVHS HDTAHILGEE GVMVRSGDHC
SKPFMTHLSI QSCCRASFCI YNTMEDVEAL TRALHAVGRI FQCS