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Database: UniProt/TrEMBL
Entry: A0A0K2SHU5_9FIRM
LinkDB: A0A0K2SHU5_9FIRM
Original site: A0A0K2SHU5_9FIRM 
ID   A0A0K2SHU5_9FIRM        Unreviewed;       959 AA.
AC   A0A0K2SHU5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
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   ORFNames=LIP_0788 {ECO:0000313|EMBL:BAS26645.1};
OS   Limnochorda pilosa.
OC   Bacteria; Firmicutes; Limnochordia; Limnochordales; Limnochordaceae;
OC   Limnochorda.
OX   NCBI_TaxID=1555112 {ECO:0000313|EMBL:BAS26645.1, ECO:0000313|Proteomes:UP000065807};
RN   [1] {ECO:0000313|Proteomes:UP000065807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HC45 {ECO:0000313|Proteomes:UP000065807};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence and phylogenetic analysis of Limnochorda
RT   pilosa.";
RL   Submitted (JUL-2015) 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: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; AP014924; BAS26645.1; -; Genomic_DNA.
DR   RefSeq; WP_068134500.1; NZ_AP014924.1.
DR   EnsemblBacteria; BAS26645; BAS26645; LIP_0788.
DR   KEGG; lpil:LIP_0788; -.
DR   PATRIC; fig|1555112.3.peg.819; -.
DR   KO; K01595; -.
DR   Proteomes; UP000065807; 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:UP000065807};
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:BAS26645.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065807}.
FT   ACT_SITE    164    164       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    618    618       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   959 AA;  107684 MW;  0FC73D852C300AB7 CRC64;
     MNDLARNLVP GPARPGEAPI QWRPQDRPLR RDVHILADML MHILAEEVSP RLAEQVEGLR
     RTCKALREGA SPELEHQLEA SISALPQEEA LRLIRAFSLY FQLVNLAEER HRARRRRQYR
     LDRPTGQAGS PEDLAVHLRE AGVGPEQLQQ VLNRLRITLV TTAHPTQTLR RTVIDHHQRI
     AALLERLDDP RLVPAERRRV LEGLRQEIRL LWQTDELRER RPTVLDEVRE GLFYFERTLL
     EVAPRLLAEL ERALNDAYPG ASLRVPGILR FGTWIGGDRD GNPRVTPEVT RRALLAQKRL
     VITRYLQHLD RLGSRMSQSV RLASVPPGLT ELLESYRAAF PDVYRWAAGR FPGEPFREAW
     VYARWRLELA RPPADPEGVA DLDSFSPFRG EPPAPADPRG YPNAAAFLDD LHRIQEALGA
     TSPARPHLDE LDLFIRQVEL FGFHLAAMDV REDGARVRRA ARSLLEAAGL RPPTSPADWN
     RLLAGPPLLG EPASAGSGVD PELAEILESL RVIRWAQEAI DPPAACAYLI SMVHGPEALW
     EALLLAREAG LFRWEPAPGE HPPAESRVDV VPLVESIGDL RRAGAILEGA WTLPAYQAQL
     SARGNHQEVM LGYSDSNKDG GYFTSNWEIY QAQRRLMQAA RRRGVEITFF HGRGGAIGRG
     GGPSVKALMG LPPGSLPGAM RITEQGEVLS SRYLQPELAM RNLEQLATAA IWSSVPQARM
     PAARTVGAHS AWEEAADRLS QLALATYRGL VERPGFEAYF RQATPIAYVE RLKIGSRPSS
     RPDMEEMEGL RAIPWVFAWT QSRHLIPGWY GVGTALERFA TESPENLALL QEMAQAWAFW
     QPLMDNLEMA MCKADLGVAR LYARLAPEGK EFLDLIEDEF RRTREWVLRL SGRSELLDGQ
     PVLQRSIRLR NPYVDPLSYL QVEMIRRHRA ASPPEEQAVL EDAIFRSING VVGGLRNSG
//
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