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Database: UniProt/TrEMBL
Entry: Q0I065_SHESR
LinkDB: Q0I065_SHESR
Original site: Q0I065_SHESR 
ID   Q0I065_SHESR            Unreviewed;       889 AA.
AC   Q0I065;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-SEP-2017, entry version 88.
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=Shewmr7_0235 {ECO:0000313|EMBL:ABI41240.1};
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI41240.1, ECO:0000313|Proteomes:UP000001960};
RN   [1] {ECO:0000313|Proteomes:UP000001960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7 {ECO:0000313|Proteomes:UP000001960};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI41240.1; -; Genomic_DNA.
DR   RefSeq; WP_011624811.1; NC_008322.1.
DR   ProteinModelPortal; Q0I065; -.
DR   EnsemblBacteria; ABI41240; ABI41240; Shewmr7_0235.
DR   KEGG; shm:Shewmr7_0235; -.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001960; 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   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:UP000001960};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABI41240.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABI41240.1}.
FT   ACT_SITE    146    146       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    553    553       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   889 AA;  100223 MW;  87B153E5A878E88B CRC64;
     MAGNVADNVT DMYASLRSNV SMLGQILGDT MRTHLGDSFL EKVEQIRKLA KDSRRGDEAA
     REQMLELLTA LPDEELVPFA KAFNQFLNLA NLSEQFHTIS RNCDELVCVP DPVEQLLGRM
     LNGRIDQTKM LDCLKTLDID LVLTAHPTEI SRRTLIQKYA AIVDCLAEQE NNQLSDRERR
     QINLRLRQLI AQIWHTNEIR RERPTPVDEA RWGLSTIEES LWHAVPDFLR QLNDQVQDRT
     GQQLPIDIAP VRFSSWMGGD RDGNPFVTAK VTQEVLDRNR HAAARLFLKD IVLLVGELSM
     EEANSELMAF TNNSCEPYRF VLRSLRQKLR DTIDYLNARI EGHNPEVDKS TLIWQESDLK
     APLEMLYKSL CDCGMRLIAN GLLLDILRRL ACFGIHMLRL DIRQDAGRHC DVLAELTRYL
     GMGDFNHWDE TEKQAFLLRE LSNRRPLIPS NWQPSADVAE VLNTCRLIAK HPAKALGSYV
     ISMASKPSDV LTVLLLLKET GCTHPMRVVP LFETLSDLNN AAECITALLD IDWYRGYTKG
     MQEVMIGYSD SAKDAGVMAA AWAQYRAQEQ LVAVCQQAGV KLTLFHGRGG SIGRGGGPAH
     KAILSQPPGS VDGRIRVTEQ GEMIRFKFGL PKLAVQSLAL YTSAVLEATL LPPPEPKQEW
     RNCVERIAEE SVSAYRGIVR EEPDFVPYFR AATPEVELGK LPLGSRPAKR RVDGGIESLR
     AIPWIFAWSQ NRLMLPAWLG AGEALQAACQ RGEIGLLQDM EREWPFFSTR ISMLEMVYAK
     AEPNLARYYE TCLVPPNLHH LGETLRQRLD LGIKVVLELT KSDTLMAHTP WNRESVKLRN
     PYIDPLNFLQ TELLARTRKE TTEAPASEHV QLALMLTIAG VAAGMRNTG
//
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