(data stored in SCRATCH zone)

SWISSPROT: Q145S2_PARXL

ID   Q145S2_PARXL            Unreviewed;       270 AA.
AC   Q145S2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   SubName: Full=Citrate lyase {ECO:0000313|EMBL:ABE28917.1};
GN   ORFNames=Bxe_A4082 {ECO:0000313|EMBL:ABE28917.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28917.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28917.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28917.1,
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   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|SAAS:SAAS00571010}.
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DR   EMBL; CP000270; ABE28917.1; -; Genomic_DNA.
DR   RefSeq; WP_011486744.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4082; -.
DR   EnsemblBacteria; ABE28917; ABE28917; Bxe_A4082.
DR   GeneID; 4003383; -.
DR   KEGG; bxb:DR64_1758; -.
DR   KEGG; bxe:Bxe_A4082; -.
DR   PATRIC; fig|266265.5.peg.401; -.
DR   eggNOG; ENOG4105CI0; Bacteria.
DR   eggNOG; COG2301; LUCA.
DR   HOGENOM; HOG000242281; -.
DR   KO; K01644; -.
DR   OMA; NAVGTPW; -.
DR   OrthoDB; 1107373at2; -.
DR   BioCyc; BXEN266265:BXE_RS01905-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145S2.
DR   SWISS-2DPAGE; Q145S2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Lyase {ECO:0000313|EMBL:ABE28917.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2,
KW   ECO:0000256|SAAS:SAAS00460587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        4    209       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       116    116       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       142    142       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      63     63       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     116    116       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   270 AA;  29116 MW;  4734F24B45C32120 CRC64;
     MDARSYLFVP GDRPERFAKA LGTGADAVVI DLEDAVVPAA KLAARDGLRR WLPTVDPARL
     IVRVNAVGTP WHLEDVEMVR ASGVSVMMLP KSDSARQLAE VAARLPSTVR IVALIETVAG
     VVAMREIAGV PSVARLAFGT VDFCGDAGIE GLGAELDYVR SQMVIESRYA GLAAPIDGVT
     PELDHLERLT EHVAGARRFG FGGKLCIHPR QVEPVNRGFA PSEDERRWAA RVLAACSEHP
     EGAFAVDGKL VDRPVIERAK KIAEFDTLIH
//

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