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Database: UniProt/TrEMBL
Entry: I0BU89_9BACL
LinkDB: I0BU89_9BACL
Original site: I0BU89_9BACL 
ID   I0BU89_9BACL            Unreviewed;       929 AA.
AC   I0BU89;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   20-DEC-2017, entry version 42.
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=B2K_35425 {ECO:0000313|EMBL:AFH65936.1};
OS   Paenibacillus mucilaginosus K02.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH65936.1, ECO:0000313|Proteomes:UP000007392};
RN   [1] {ECO:0000313|EMBL:AFH65936.1, ECO:0000313|Proteomes:UP000007392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K02 {ECO:0000313|EMBL:AFH65936.1,
RC   ECO:0000313|Proteomes:UP000007392};
RA   Xiao B., Sun L., Xiao L., Lian B.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL   Submitted (JUN-2013) 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; CP003422; AFH65936.1; -; Genomic_DNA.
DR   RefSeq; WP_013921116.1; NC_017672.3.
DR   EnsemblBacteria; AFH65936; AFH65936; B2K_35425.
DR   KEGG; pmw:B2K_35425; -.
DR   PATRIC; fig|997761.3.peg.7143; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000007392; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007392};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AFH65936.1}.
FT   COILED      312    332       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    153    153       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    586    586       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   929 AA;  106165 MW;  C9A774ABF79922D2 CRC64;
     MSDSVSLIHK NTSNNLLRRD VRFLGHILGE VLVHQGGNAL FTIVEKIREM SKTLRADYTP
     EMYAELKETV TGLAPEIRHQ VIRAFAVYFQ LINIAEQNHR IRRKRDYERT AGENVQPGSI
     EDSVRELKSL GISSDEVQEM IQGISLELVM TAHPTEATRR AVLDIHQRIA GDVMELDNPN
     LTFREREQLR EKLLGEVITL WQTDELRDRK PTVIDEVRNG LYYFDETLFD VLPEVYQELE
     RCLDKYYPEE DWHVPTYLKF GSWIGGDRDG NPSVKASVTW ETLTMHRKLA LAKYEEELTG
     LLEHMSFSRS IVEVSEELLE SIEKDRREIE LSSDNEWRNL KEPYRIKVKF MTERIRNTGN
     PNAPAKRKYN NPDEFRADLQ IIERSLRNHY ADFIADTYVQ KLVRQVELFG FHLAALDVRQ
     HSKEHEAAMT EILAKMSICE DYSKLPEAEK IELLTAILND PRPITSPYLR YSESTQECLD
     VYRVIQKAQQ EFGRSCISSY LISMTQGASD LLEVLVFGKE AGLYIHENDG SITCTLQSVP
     LFETIDDLHA APDIMTTLFK IPAYRNSLVS TNHLQEIMLG YSDSNKDGGV ITANWELRVA
     LRGITAAAKP FDVKLKFFHG RGGALGRGGM PLNRSILAQP ADTVGGGIKI TEQGEVLSSR
     YSMKGIAYRS LEQATSALIT SALQARNPQT NASEAEWENI MRGISEQAQT KYQDLIFRDE
     DFLTFFKEST PLPEIGELNI GSRPSKRKNS DRFEDLRAIP WVFAWTQSRY LLPAWYAAGY
     GLNSFYAGKK ENLQKMQEMY QNWSFFRSLI DNLQMALAKA DLLIAKEYGS MIQDQSIAER
     IFGLIQDEYT RTSELILNIT GQQEILDNVP VIQESIRLRN PYVDPLSYMQ VGLLSELRTL
     RDQGEDDALL LREVLLTING IAAGLRNTG
//
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