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Database: UniProt/TrEMBL
Entry: Q0K7M4_CUPNH
LinkDB: Q0K7M4_CUPNH
Original site: Q0K7M4_CUPNH 
ID   Q0K7M4_CUPNH            Unreviewed;      1012 AA.
AC   Q0K7M4;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-SEP-2017, entry version 83.
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   ECO:0000313|EMBL:CAJ93997.1};
GN   OrderedLocusNames=H16_A2921 {ECO:0000313|EMBL:CAJ93997.1};
OS   Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
OS   (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ93997.1, ECO:0000313|Proteomes:UP000008210};
RN   [1] {ECO:0000313|EMBL:CAJ93997.1, ECO:0000313|Proteomes:UP000008210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337
RC   {ECO:0000313|Proteomes:UP000008210};
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
RA   Cramm R., Eitinger T., Ewering C., Potter M., Schwartz E.,
RA   Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
RA   Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium
RT   Ralstonia eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
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; AM260479; CAJ93997.1; -; Genomic_DNA.
DR   RefSeq; WP_010813833.1; NC_008313.1.
DR   ProteinModelPortal; Q0K7M4; -.
DR   STRING; 381666.H16_A2921; -.
DR   EnsemblBacteria; CAJ93997; CAJ93997; H16_A2921.
DR   KEGG; reh:H16_A2921; -.
DR   PATRIC; fig|381666.6.peg.3317; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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; IPR033129; PEPCASE_His_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.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008210};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CAJ93997.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CAJ93997.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008210}.
FT   ACT_SITE    215    215       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    662    662       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1012 AA;  112160 MW;  D5765D8914ECE8D1 CRC64;
     MTQHAARPNG RRTAPAAKDQ SPALGAAQGD ANGASAAEPK RPASRSGTKR SPKPKLSIVS
     SNGTTIAPTA RRTADKDVPL REDIRFLGRL LGECLREQEG DAAFEVVETI RQTAVRFRRE
     NDRAAGAELD RLLKRLSRDQ TNQVVRAFSY FSHLANIAED QHHNRRRRVH ALAGSPPQAG
     SLAHALEAID AAGVTGKQLR KFLDEALIVP VLTAHPTEVQ RKSILDAERE IARLLAERDL
     PMTARERDHN TAQLRAKVTT LWQTRMLRDS RLTVADEIEN ALSYYRTCFL RGIPQLMSEL
     EEDIAAVFPT TRKRKGTPGA QPAPLAPFLQ MGSWIGGDRD GNPNVTAETL EHAASQQGQM
     IIDWYLDEVH ALGAELSMST LMVDASPELL ALAERSPDHS EHRADEPYRR ALIGIYARLA
     ATSKALTGHA VPRRPVAPAE PYDSAEAFAA DVQVVVDSLR ANHGQALANG RIEALARAIG
     VFGFHLASVD MRQVSDVHEA VIAELFAAAG IAPDYAALPE ARKLELLLAE LRQPRLLTLP
     WHEYSEQTRK ELAIFAAARE LRARYGKRIA RNYIISHTET LSDLVEVMLL QKESGMLQGT
     LGSKTDPARM ELMVIPLFET IEDLRNAAGI MQSLLDLPGF DSVIAHHGVE QEVMLGYSDS
     NKDGGFLTST WELYKAELEL VQLFEQRQVK LRLFHGRGGT VGRGGGPTYQ AILSQPPGTV
     NGQIRLTEQG EIINSKFANA EIGRRNLETV VAATLEASLL PQQNAPKDLD MFEAVMQQLS
     DRAFTAYRDL VYETPGFKDY FFATTPITEI ADLNLGSRPA SRKLMDKKNR RIEDLRAIPW
     GFSWGQCRLL LPGWYGFGSA VKSLLDTAPD DKARKLAVTT LRRMVKTWPF FSTLLSNMDM
     VLAKTDLAVA SRYAQLCDDA ALRRTVFNRI SKEWHLTCEM LTLVTGHQER LADNPLLARS
     IKNRFAYLDP LNHLQVELLK RYRSGKDGDD IRVRRGIHLT INGVAAGLRN TG
//
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