CSD_ALKHC
ID CSD_ALKHC Reviewed; 406 AA.
AC Q9K7A0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; OrderedLocusNames=BH3469;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(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 -!- SEQUENCE CAUTION:
CC Sequence=BAB07188.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BA000004; BAB07188.1; ALT_FRAME; Genomic_DNA.
DR PIR; E84083; E84083.
DR AlphaFoldDB; Q9K7A0; -.
DR SMR; Q9K7A0; -.
DR STRING; 272558.10176092; -.
DR EnsemblBacteria; BAB07188; BAB07188; BAB07188.
DR KEGG; bha:BH3469; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_5_2_9; -.
DR OMA; HKLCGPT; -.
DR Proteomes; UP000001258; 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; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150292"
FT ACT_SITE 361
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 44632 MW; 35FB20313CCA24FB CRC64;
MNAHEIKKLF PVLDQEVNGS PLVYLDSAAT SQKPIAVIEA LDDYYRRYNS NVHRGVHTLG
TLATDGYEGA REKIRRFIHA SSTEEIIFTR GTTTAINLVA ASYGRANLGE GDEIVITPME
HHSNIIPWQQ VAKATGATLT YLPLQKDGTI KIEDVEKTIS EKTKIVAIMH VSNVLGTINP
VKEIAEIAHR HGAIMLVDGA QSAPHMKIDV QELGCDFFAF SGHKMAGPTG IGVLYGKKAH
LEKMEPVEFG GEMIDFVGLY DSTWKELPWK FEGGTPIIAG AIGLGAAIDF LEDIGLDEIE
KHEHELAQYA LDRLSELEGM TVYGPQKRAG LVTFNIEDVH PHDVATVLDA DGIAVRAGHH
CAQPLMKWLD VTATARASFY LYNTKEDIDA LAKGLEKTKE YFGHVF
