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Database: UniProt/TrEMBL
Entry: A0A089PD94_9PROC
LinkDB: A0A089PD94_9PROC
Original site: A0A089PD94_9PROC 
ID   A0A089PD94_9PROC        Unreviewed;       994 AA.
AC   A0A089PD94;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-NOV-2017, entry version 21.
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   ORFNames=EW15_2094 {ECO:0000313|EMBL:AIQ98186.1};
OS   Prochlorococcus sp. MIT 0801.
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=1501269 {ECO:0000313|EMBL:AIQ98186.1, ECO:0000313|Proteomes:UP000029485};
RN   [1] {ECO:0000313|EMBL:AIQ98186.1, ECO:0000313|Proteomes:UP000029485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 0801 {ECO:0000313|EMBL:AIQ98186.1,
RC   ECO:0000313|Proteomes:UP000029485};
RA   Biller S., Berube P., Thompson J., Kelly L., Roggensack S., Awad L.,
RA   Roache-Johnson K., Ding H., Giovannoni S.J., Moore L.R.,
RA   Chisholm S.W.;
RT   "Genomes of diverse isolates of the marine cyanobacterium
RT   Prochlorococcus.";
RL   Submitted (JUL-2014) 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}.
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; CP007754; AIQ98186.1; -; Genomic_DNA.
DR   RefSeq; WP_038654403.1; NZ_CP007754.1.
DR   EnsemblBacteria; AIQ98186; AIQ98186; EW15_2094.
DR   KEGG; prm:EW15_2094; -.
DR   KO; K01595; -.
DR   Proteomes; UP000029485; 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:UP000029485};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AIQ98186.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AIQ98186.1}.
FT   ACT_SITE    178    178       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    634    634       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   994 AA;  113198 MW;  FB60DE5FF92A5DD6 CRC64;
     MLKNPSNENI SNHSTVCVED QDPGSLLQQR LELVEDLWKT VLKSECPPDQ TERLLRLKQL
     SDPSKSNQDN SSQAIVQLIT KMDLAEAISA ARAFSLYFQL VNILEQRIEE DSYLESIEKG
     KLDNSNSQID PFAPALASQT APATFTQLFE RLRRLNVPPA QLDGLMREMD IRLVFTAHPT
     EIVRHTVRHK QRRVATLLQQ LQSNSLISES EKEIFRLQLE EEIRLWWRTD ELHQFKPTVL
     DEVDYALHYF QQVLFDAMPQ LRRRLTTALA SSYPDVEIPN EAFCTFGSWV GSDRDGNPSV
     TPEITWRTAC YQRQLMLDRY IASVQELRDQ LSISMQWSQV SSPLLESLEM DRVRFPDVYE
     ERAARYRLEP YRLKLSYTLE RLRLTQLRNK QLADAGWQFS PDGKPLISTD NSFDEFLHYK
     SVDELKNELE LIRNSLVSTD LTCEPLDTLL NQVHIFGFSL ASLDIRQEST RHSDALDELT
     CYLDLPESYG AMSEESRVQW LMKELKTRRP LIPPAFEWSK STQETISVFH MLHRLQKEFG
     TRICRSYVIS MSHTASDLLE VLLLAKESGL IDPTLGASDF LVVPLFETVE DLQHAPSVME
     SLLQTDVYRE LLPRVGEKKQ PLQELMLGYS DSNKDSGFLS SNWEIHKAQI ALQDLASRQG
     IALRIFHGRG GSVGRGGGPA YQAILAQPSG TLQGRIKITE QGEVLASKYS LPELALYNLE
     TVTTAVIQNS LVTNKLDATP SWNELMTRLA ARSREHYRAL VHDNPDLVQF FQVVTPIEEI
     SKLQISSRPA RRKSGAKDLS SLRAIPWVFG WTQSRFLLPS WFGVGTALAT ELKTDPDQME
     MLRMLNQRWP FFRMLISKVE MTLSKVDLDV AHHYMVSLGG GDDRDAFAAI FDIISSEYTL
     TKKLILEITD KSKLLSADPA LQLSVNLRNR TIVPLGFLQV ALLKRLRDQN RQPPISEDMS
     SDSTQSSRTY SRSELLRGAL LTINGIAAGM RNTG
//
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