(data stored in ACNUC7421 zone)

SWISSPROT: C7QHJ4_CATAD

ID   C7QHJ4_CATAD            Unreviewed;       940 AA.
AC   C7QHJ4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Caci_0178 {ECO:0000313|EMBL:ACU69133.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69133.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69133.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP001700; ACU69133.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0178; -.
DR   EnsemblBacteria; ACU69133; ACU69133; Caci_0178.
DR   KEGG; cai:Caci_0178; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QHJ4.
DR   SWISS-2DPAGE; C7QHJ4.
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ACU69133.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ACU69133.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   ACT_SITE    163    163       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    596    596       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   940 AA;  103424 MW;  85BA88D7CC310BC4 CRC64;
     MSAVPSPKND DAAVETPTDS PTARANDTAN DNPPRTADDA ELRAAIRRLG DLLGQTLVRQ
     HGPELLEQVE AIRALGKQGA DVSELLAAVD PEQAIKLVRA FTAYFNLANT AEQVHRGREL
     AATRAAEGSW LGQAVDRIQA AGLAGTAAEA VSHLSVRPVF TAHPTEAARR TVLAKLRKVA
     ELLEAPQTAY NERRLAETVE QLWQTDEIRI TRPEPVDEAR NAVYYLDELA AHAAPEVLEE
     LAVELRRLGV ELPLSARPLS FGSWIGGDRD GNPNVTPQMT LDVLELQHEH AIRTALASMD
     ALREILSTSE RIAAPTEALR ASLDADLEAL PEIPNRYRRL NAEEPYRLKA TTIRQKLLNT
     RTRIAEGRQH DPRRDYLGTS ELLRDLSLMR DSLYADRGEL IATGELETAI RTIAAFGLHH
     AVLDVREHAD AHHHVLAQLF DRLGDQPWRY SDLPRDYRTR LLAKELASSR PLSALGQVPA
     DTLLDAAGVK SFGVFTAIRT AFEKYGPDVI ESYIVSMTRG VDDLFAAVVL AREAGLVDVH
     AHTAAIGFVP LLETPDELKI AGSILDEMLS DPSYAAIVAA RGGVQEVMLG YSDSNKMGGI
     STSQWEIHRA QRELRDTALR HGIRIRLFHG RGGSVGRGGG PSHDAILAQP WGTLDGEIKV
     TEQGEVISDK YAIPALAREN LELTLAATLE ATVLHRAPRQ SAEDLATWSA TMEGVSSAGQ
     DRYRELVEHP DLPAYFFAST PVDLLGDLHL GSRPSRRPDT SAGIDGLRAI PWVFGWTQSR
     QIVPGWFGVG TGLAAARQNP AFAGTDWQDM YERWHFFRNF LGNVSMTLAK TDLRIARHYV
     ETLVPRELHH FFDTITEEYE RTVAEVLRIT GESELLGRNE TLARTLRVRD MYLDPISYMQ
     VSLLKRQREA TKAGLPVDPD LARALLLSVN GIAAGLKNTG
//

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