(data stored in SCRATCH zone)

SWISSPROT: Q3KJR7_PSEPF

ID   Q3KJR7_PSEPF            Unreviewed;       334 AA.
AC   Q3KJR7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   SubName: Full=D-cysteine desulfhydrase {ECO:0000313|EMBL:ABA71989.1};
DE            EC=4.4.1.15 {ECO:0000313|EMBL:ABA71989.1};
GN   OrderedLocusNames=Pfl01_0245 {ECO:0000313|EMBL:ABA71989.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71989.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71989.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71989.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00339553};
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000256|SAAS:SAAS00536520}.
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DR   EMBL; CP000094; ABA71989.1; -; Genomic_DNA.
DR   RefSeq; WP_011331949.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0245; -.
DR   PRIDE; Q3KJR7; -.
DR   EnsemblBacteria; ABA71989; ABA71989; Pfl01_0245.
DR   KEGG; pfo:Pfl01_0245; -.
DR   eggNOG; ENOG4105K6H; Bacteria.
DR   eggNOG; COG2515; LUCA.
DR   HOGENOM; HOG000022459; -.
DR   KO; K05396; -.
DR   OMA; AKIGMKC; -.
DR   BioCyc; PFLU205922:G1G4S-246-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0019148; F:D-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005966; D-Cys_desShydrase.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01275; ACC_deam_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJR7.
DR   SWISS-2DPAGE; Q3KJR7.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Lyase {ECO:0000313|EMBL:ABA71989.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR006278-2,
KW   ECO:0000256|SAAS:SAAS00006054}.
FT   DOMAIN       19    322       PALP. {ECO:0000259|Pfam:PF00291}.
FT   COILED      129    149       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     82     82       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006278-1}.
FT   MOD_RES      55     55       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR006278-2}.
SQ   SEQUENCE   334 AA;  35560 MW;  CC955273A16A5AEF CRC64;
     MSTQPIKQQL QRFNRLDLLG QPTPLEKLER LSTWLGRDVY IKRDDLTPLA MGGNKLRKLE
     YLAADAIAQG ADTLITAGAL QSNHVRQTAA LAAKLGLGCV ALLENPLGTD DSNYTGNGNR
     LLLDLFDTKV ELVDNLDNAD EQLAALAVRL RSNGKKPYLV PIGGSNAIGA LGYVRAGLEL
     AEQIKDTGLQ FSAVVLASGS AGTHSGLALA LSEALPQLPV IGVTVSRSEE DQRPKVQGLA
     ERTADLLGVA LPDSFKVELW DEYFGPRYGE PNAGTLSAVK LLASQDAVLL DPVYTGKAMA
     GLLDGIGRGR FDDGPIIFLH TGGAPALFAY KDFL
//

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