CSD_PSEAE
ID CSD_PSEAE Reviewed; 401 AA.
AC Q9HXX3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; OrderedLocusNames=PA3667;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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}.
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DR EMBL; AE004091; AAG07055.1; -; Genomic_DNA.
DR PIR; F83187; F83187.
DR RefSeq; NP_252357.1; NC_002516.2.
DR RefSeq; WP_003098634.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXX3; -.
DR SMR; Q9HXX3; -.
DR STRING; 287.DR97_4210; -.
DR PaxDb; Q9HXX3; -.
DR PRIDE; Q9HXX3; -.
DR EnsemblBacteria; AAG07055; AAG07055; PA3667.
DR GeneID; 880538; -.
DR KEGG; pae:PA3667; -.
DR PATRIC; fig|208964.12.peg.3836; -.
DR PseudoCAP; PA3667; -.
DR HOGENOM; CLU_003433_2_5_6; -.
DR InParanoid; Q9HXX3; -.
DR OMA; PVCLRYG; -.
DR PhylomeDB; Q9HXX3; -.
DR BioCyc; PAER208964:G1FZ6-3737-MON; -.
DR Proteomes; UP000002438; 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 PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150307"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 401 AA; 43274 MW; AB944EFD7E64699B CRC64;
MSLPSPWRAD FPAFSAFAAE GLTYLDSAAT AQKPQAVLDA LNGYYLGGAA NVHRAQHVPG
ERATRAFEAA RSRVAHWLHA GNPAEVLFTR GTTEAINLVA YGLERHFRPG DELLVSALEH
HANLLPWQQL ALRRGLVLRV LPLDERGVID LEQARHIIGE RTRLLAISQL SNVLGTWQPV
VELIQLARER GAWTLVDGAQ GSVHGRHDLP GLGCDFYAFS GHKLYGPDGI GVLWGRPQAL
EQLAHWQFGG EMVRHTGFHE ASFHAAPLGF EAGTPAVSAA IGLGATIDWL ATLDEAEVAA
HEGALHARLL AGLLARDGVS LLGEPQAALA SFCVDGVHVA DLAHLLGEQG IAVRAGHHCA
MPLLQRLEVP GALRVSLGLY NDADDLERFF LALDRSLELL R