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Database: UniProt/TrEMBL
Entry: A0A1C9W698_9GAMM
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Original site: A0A1C9W698_9GAMM 
ID   A0A1C9W698_9GAMM        Unreviewed;       887 AA.
AC   A0A1C9W698;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   22-NOV-2017, entry version 8.
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:AOS96658.1};
GN   ORFNames=AUP74_01196 {ECO:0000313|EMBL:AOS96658.1};
OS   Microbulbifer aggregans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=1769779 {ECO:0000313|EMBL:AOS96658.1, ECO:0000313|Proteomes:UP000095672};
RN   [1] {ECO:0000313|EMBL:AOS96658.1, ECO:0000313|Proteomes:UP000095672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-MM1 {ECO:0000313|EMBL:AOS96658.1,
RC   ECO:0000313|Proteomes:UP000095672};
RA   Moh T.H., Dinesh B., Lau N.-S., Go F., Alexander Chong S.-C.;
RT   "Complete genome sequence of Microbulbifer sp. CCB-MM1, a halophile
RT   isolated from Matang Mangrove Forest, Perak.";
RL   Submitted (JAN-2016) 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: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; CP014143; AOS96658.1; -; Genomic_DNA.
DR   RefSeq; WP_069946771.1; NZ_CP014143.1.
DR   EnsemblBacteria; AOS96658; AOS96658; AUP74_01196.
DR   KEGG; micc:AUP74_01196; -.
DR   PATRIC; fig|1769779.3.peg.1218; -.
DR   KO; K01595; -.
DR   Proteomes; UP000095672; 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:UP000095672};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AOS96658.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AOS96658.1}.
FT   ACT_SITE    144    144       {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   887 AA;  99397 MW;  B2D00B73E1F5C452 CRC64;
     MSADQNAPLR DDVRLLGEEL GSVLKAQAGE QLFDTVETIR QAAVESSDSK EVLVGRLRDL
     LDPLDDETLL EVARAFSQFL NLANIAEQRH RERLRRHHQR YPGDPDTDQS LRQVLAELKK
     SGVSQERVLS TLSDLSVELV LTAHPTEVTR RTLIRKYDQI ADLLADMDRP DLTQEEASEL
     RRHLSEQILS AWSTDEIRRE RPTPVDEAKW GFATIEQSLW HAVPQGMREI EAELDLAGLE
     SMPADWVPIR FASWMGGDRD GNPNVTAAVT REVLTLARWM AADLYLRDVE NLLADLSMHR
     ASDELLARTG PTHEPYRLLL RQVRDRLRTT RAQMEARVHS QPEPEGESYT SSAQLAEELR
     LIDRSLRAVG LSAIADGQLK DTLRRLNCFG ITLLRLDIRQ ESTRHMAALD AVTRYLGLGS
     YADWDESQKQ QFLLAELEGR RPLVDEAFYR SEFCDEEVRE VLATCRVIAE QGSEGLGAYV
     ISMAKTSSDV LAVMLLQKIA GVLEPMRVVP LFETLDDLNN AADTMGALLQ IPLYKERVSS
     GQEVMIGYSD SAKDAGFLGA AWAQFRAQER LTASFREHGI PLTLFHGRGG SISRGGSPTR
     MALLSQPPGS VAGRIRVTEQ GEMIRFKYGR PSVAAYNLEQ YVAATLEATL MPPAEPRPEW
     RQEMEQLTQV SVAGYRDVVR DDPALVAYLR TVTPETELSR LALGSRPARR KPGGGVETLR
     AIPWVFAWTQ IRLMLPAWLG TGAALESALA SPSETDTLRA MSEQWPFFQG VVDMLEMVLA
     KADTRVASWY EERLTDDVEL MRLGKALRER LAHTVDALQQ LTGRESLLDN NPVMRWSIRV
     RDPYTDPLHL LQAELMARLR ERDSDPVLES ALMVTIAGIA AGMRNTG
//
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