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Database: UniProt/TrEMBL
Entry: H8W7M6_MARHY
LinkDB: H8W7M6_MARHY
Original site: H8W7M6_MARHY 
ID   H8W7M6_MARHY            Unreviewed;       881 AA.
AC   H8W7M6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   28-MAR-2018, entry version 40.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CCG94474.1};
GN   ORFNames=MARHY0994 {ECO:0000313|EMBL:CCG94474.1};
OS   Marinobacter hydrocarbonoclasticus ATCC 49840.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1163748 {ECO:0000313|EMBL:CCG94474.1, ECO:0000313|Proteomes:UP000007884};
RN   [1] {ECO:0000313|EMBL:CCG94474.1, ECO:0000313|Proteomes:UP000007884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49840 {ECO:0000313|EMBL:CCG94474.1};
RX   PubMed=22689231; DOI=10.1128/JB.00500-12;
RA   Grimaud R., Ghiglione J.F., Cagnon C., Lauga B., Vaysse P.J.,
RA   Rodriguez-Blanco A., Mangenot S., Cruveiller S., Barbe V., Duran R.,
RA   Wu L.F., Talla E., Bonin P., Michotey V.;
RT   "Genome Sequence of the Marine Bacterium Marinobacter
RT   hydrocarbonoclasticus SP17, Which Forms Biofilms on Hydrophobic
RT   Organic Compounds.";
RL   J. Bacteriol. 194:3539-3540(2012).
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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; FO203363; CCG94474.1; -; Genomic_DNA.
DR   EnsemblBacteria; CCG94474; CCG94474; MARHY0994.
DR   KEGG; mhc:MARHY0994; -.
DR   PATRIC; fig|2743.3.peg.940; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000007884; Chromosome.
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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007884};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:CCG94474.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:CCG94474.1}.
FT   ACT_SITE    139    139       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    544    544       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   881 AA;  99588 MW;  A714CB543296D6F7 CRC64;
     MTELHSDLRE NVRLLGDLLG QSILRFPGQD CYDRIEEIRA AAKADRRQES GSGQRLVKLL
     GQLSDDELLP VTRAFNQFLN LANLAEQYHG IRRKQGHPSD LMVESLGDVF DRLKSGGIDP
     QELHRKVADL RIEFVLTAHP TEVARRTLIL KYDEMSDCLS RLDHDDLMPG EREEIVDRLS
     LLIAEAWHTD EIRHERPTAV DEAKWGFAVI ENSLWQALPK FLRSLDTSLS EATGQGLPLQ
     VSPIRIASWM GGDRDGNPNV THEVTREVFL LGRWMAADLY LRDIQALRAE LSMWQASDEL
     RAEVGDSREP YRQVLAQLRE RLIKTRDWAE ASVKGEPADD SGILFENEDL TGPLELCYRS
     LMECGLETIA NGPLLDTIRR AHTFGLPLIR LDIRQEASRH AEAVAEMVNY LGLGDYLSWS
     EQERQAFLVK ELKGRRPLVP RNWQPSEPVR EVLATCEVVA GQTPEALGSY VISMASKPSD
     VLNVILLLRE AGMAFPMRVV PLFETLDDLK GAPDSMAALY EVDWYREYCS GRQEVMIGYS
     DSSKDAGQLM AAWAQYQAQE KLTEVANRYG VHLTLFHGRG GTVGRGGGPA NRAILSQPPG
     SVNGSFRITE QGEMIRFKFG LPRLAVQSLT LYTTAVIEAT LAPPPVPKDE WREVMDWLTE
     RSLRSYREVV RENPDFVPYF RQVTPETALG KLALGSRPAR RKATGGVESL RAIPWIFAWT
     QMRLMLPSWL GSDVALEQAA QADRLPELRE MMQGWPFFRT YVDMLEMVLA KADLRIASYY
     EQTLVEDEHL LALGQSLRQR LQGCIERLLE LKQQQTLLEQ EPVFAHSMKV RNPYTDPLHY
     LQAELLRRDR ESEGAGKVPE LVERALKVTM AGISAGMRNT G
//
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