(data stored in SCRATCH zone)

SWISSPROT: Q13IP0_PARXL

ID   Q13IP0_PARXL            Unreviewed;       688 AA.
AC   Q13IP0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|SAAS:SAAS00062216};
DE            EC=2.8.1.7 {ECO:0000256|SAAS:SAAS00062216};
GN   ORFNames=Bxe_C0124 {ECO:0000313|EMBL:ABE36049.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36049.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36049.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36049.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH +
CC         L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737,
CC         Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7;
CC         Evidence={ECO:0000256|SAAS:SAAS01122505};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00170368};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|SAAS:SAAS00561004}.
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DR   EMBL; CP000272; ABE36049.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_C0124; -.
DR   EnsemblBacteria; ABE36049; ABE36049; Bxe_C0124.
DR   KEGG; bxe:Bxe_C0124; -.
DR   eggNOG; ENOG4105C9B; Bacteria.
DR   eggNOG; COG0520; LUCA.
DR   HOGENOM; HOG000017511; -.
DR   KO; K11717; -.
DR   OMA; RENSNIH; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13IP0.
DR   SWISS-2DPAGE; Q13IP0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Lyase {ECO:0000313|EMBL:ABE36049.1};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00446889};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|SAAS:SAAS00062250,
KW   ECO:0000313|EMBL:ABE36049.1}.
FT   DOMAIN      308    677       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   688 AA;  71279 MW;  256D2DE08782FDCD CRC64;
     MDSVLPHDVP SGPPAGLPDP ALLATLANAF FSALPGSAPQ PDGGGVVGGA PSLAGTLPLS
     APVLGELSNP VPAGSPLAGP GGAGTGVPGA ALPQGRLPGG NLLPSAPTHV LSLGNRAPAL
     APHAAAQNGL PDSAVTVAPA LAPRFGGAAL GVSEGHGAQR PSAGGAPAPS AVSSPSASPF
     YFLGDAGPAH PAAGASSDIV VPGWSEVTAQ SLGLPGVDEP LSGQRFSYDR PDEPASAANT
     HTARAAQPAG SSHYFLNEAQ ASRLPGQKSG MADAVPHAGA SAHPPFDVNA IRRDFPILQE
     RVNGRQLVWF DNAATTHKPQ AVIDRLAYFY AHENSNIHRA AHALAGRATD AYEAARSKVQ
     RFIGASSPDE VIFVRGTTEA INLIAKTWGA KNVGEGDEII VSHLEHHANI VPWQQLAAQT
     GAKLRVIPVD DSGQVLLDEY RRLLNDRTKI VSVTQVSNAL GTVVPVKEIV ELAHRAGAKA
     LVDGAQSVSH MRVDVQALDA DFFVFSGHKV FGPTGIGVVY GKRAILEDMP PWQGGGNMIA
     DVTFERTVFQ PPPNRFEAGT GNIADAVGLG AAIDYVQQVG IENIARYEHD LLAYATSVLQ
     PVPGVRLIGT ARDKASVLSF VLKGYETEEV GHALNEEGIA VRSGHHCAQP ILRRFGVEAT
     VRPSLAFYNT CDEVDALVSV VRRLSARR
//

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