(data stored in ACNUC7421 zone)

SWISSPROT: Q0SKB5_RHOJR

ID   Q0SKB5_RHOJR            Unreviewed;       278 AA.
AC   Q0SKB5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 76.
DE   SubName: Full=Citrate lyase {ECO:0000313|EMBL:ABG92021.1};
DE            EC=4.1.3.6 {ECO:0000313|EMBL:ABG92021.1};
GN   OrderedLocusNames=RHA1_ro00185 {ECO:0000313|EMBL:ABG92021.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92021.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|SAAS:SAAS00571010}.
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DR   EMBL; CP000431; ABG92021.1; -; Genomic_DNA.
DR   RefSeq; WP_009472732.1; NC_008268.1.
DR   ProteinModelPortal; Q0SKB5; -.
DR   STRING; 101510.RHA1_ro00185; -.
DR   PRIDE; Q0SKB5; -.
DR   EnsemblBacteria; ABG92021; ABG92021; RHA1_ro00185.
DR   GeneID; 4217604; -.
DR   KEGG; rha:RHA1_ro00185; -.
DR   PATRIC; fig|101510.16.peg.212; -.
DR   eggNOG; COG2301; LUCA.
DR   HOGENOM; HOG000242281; -.
DR   KO; K01644; -.
DR   OMA; THGGHPP; -.
DR   OrthoDB; POG091H08ZB; -.
DR   BioCyc; RJOS101510:GJJ1-185-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
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; Q0SKB5.
DR   SWISS-2DPAGE; Q0SKB5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Lyase {ECO:0000313|EMBL:ABG92021.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2,
KW   ECO:0000256|SAAS:SAAS00088067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN       17    215       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       126    126       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       152    152       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      73     73       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     126    126       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   278 AA;  29222 MW;  3585B0121D906A46 CRC64;
     MSVETAQRSE VGVAMARSWL LVPAVGSEVL AAAAASGADS LVIDLEDGLP FAAKDEGRAR
     TAEWLARNAG WVRINDATTP HWQRDLDAIR GLPGVRGLML SKTESPEQVR DTAEGIPGIP
     VVALVESAAA IVAADDIART APVSRLAFGI GDYCRDTGAG RTPMALAYAR SRLVNASRAA
     RIGAPIDGPT LSLDAEAVRD DTRLAREMGM TGKLTLATEQ VPVINTALAP DSNDISWAET
     TIARLGADGS RVTHGGHPPQ LARAHDILRR AAHFASRT
//

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