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Database: UniProt/TrEMBL
Entry: D4ZQG2_ARTPN
LinkDB: D4ZQG2_ARTPN
Original site: D4ZQG2_ARTPN 
ID   D4ZQG2_ARTPN            Unreviewed;      1035 AA.
AC   D4ZQG2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 48.
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:BAI94291.1};
GN   ORFNames=NIES39_Q02830 {ECO:0000313|EMBL:BAI94291.1};
OS   Arthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina
OS   platensis).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Arthrospira.
OX   NCBI_TaxID=696747 {ECO:0000313|EMBL:BAI94291.1, ECO:0000313|Proteomes:UP000006803};
RN   [1] {ECO:0000313|EMBL:BAI94291.1, ECO:0000313|Proteomes:UP000006803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-39 / IAM M-135 {ECO:0000313|Proteomes:UP000006803};
RX   PubMed=20203057; DOI=10.1093/dnares/dsq004;
RA   Fujisawa T., Narikawa R., Okamoto S., Ehira S., Yoshimura H.,
RA   Suzuki I., Masuda T., Mochimaru M., Takaichi S., Awai K., Sekine M.,
RA   Horikawa H., Yashiro I., Omata S., Takarada H., Katano Y., Kosugi H.,
RA   Tanikawa S., Ohmori K., Sato N., Ikeuchi M., Fujita N., Ohmori M.;
RT   "Genomic structure of an economically important cyanobacterium,
RT   Arthrospira (Spirulina) platensis NIES-39.";
RL   DNA Res. 17:85-103(2010).
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; AP011615; BAI94291.1; -; Genomic_DNA.
DR   RefSeq; WP_006619283.1; NC_016640.1.
DR   STRING; 696747.NIES39_Q02830; -.
DR   EnsemblBacteria; BAI94291; BAI94291; NIES39_Q02830.
DR   KEGG; arp:NIES39_Q02830; -.
DR   PATRIC; fig|696747.3.peg.4610; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006803; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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; 2.
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:UP000006803};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:BAI94291.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006803}.
FT   ACT_SITE    206    206       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    681    681       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1035 AA;  119137 MW;  8A6736301D561E53 CRC64;
     MSSLVQSSEP IPSAVVSSNA PVQASDLLLR NRLKIVEDLW ESVLRQECGE QLVDLLLQMR
     SMTSPEGQAS PHLQANVWQI IKDLDINAAI RAARAFALYF QLINIVEQHY EQREQELAYA
     QIKHQGPAES PADKSNRSIF ETRHQRFSTA EEAPVELLNQ TSRRQDDRDL ATFHNLFPML
     QRLNVPSQVI QRLLNQLDIR LVFTAHPTEI VRHTIRTKQR RIAKILQQLD TVDESYGKVD
     NTNPEATGLV KTWTGELQEQ LTEEIRLWWR TDELHQFKPT VLDEVEYSLH YFQEILFDVI
     PQLYQRIKQT LQPHFPHLKP PNYDFCKFGS WVGADRDGNP SVTPEVTWKT ACYQRGLIIN
     KYIQAVDHLN QLLSLSLHWS DVLPELLESL DRDQVQLPEV YDQVAIRYRQ EPYRLKLCYI
     LKRLENTRDR NQRLSTSNEV ERERERIVTK ENAGSLYHSG AAFLKELKLI ERNLMATGIQ
     CRDLENLICQ VEIYGFYLAR MDMRQESSVH STALNEIVDY LQLLARPYDD LTEAERTLWL
     ITELQTRRPL IPAELPFSPK TCETINTFRV MRELQQEFGQ EICQTYIISM SHDVSDLLEV
     LLLAKEAGLY DPATGIGNLQ VVPLFETVED LKKAPSVMKD LFELPLYRAM LAGGYQKYEQ
     VSQDVNASLQ EIMLGYSDSN KDSGFLSSNW EIHKAQKALQ TLAESYHISI RIFHGRGGSV
     GRGGGPAYKA ILAQPGKSIN GRIKITEQGE VLASKYSLSQ LALYNLESVA TAVIQASLLH
     TGFDEIEPWN QIMEELSVRS RSCYRALIYE QPDLVDFFEQ VTPIQEISQL QISSRPARRQ
     SDKKKDISGL RAIPWVFSWT QSRFLLPSWY GVGTAIEQFI REEPEENIKL LRYFYIKWPF
     FRTTISKAEM TLAKVDLEMA HHYVRELSHP QDRDRFEDLF QRIAKEFNLT RQMVLEITGQ
     KQLLDNDPVL QRSVRLRNGT IIPLGLLQVS LLQRLRHHGT SATPGVIHSR YSKGELLRGA
     LLTINGIAAG MRNTG
//
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