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Database: UniProt/TrEMBL
Entry: A0A0E4CZB2_9BACL
LinkDB: A0A0E4CZB2_9BACL
Original site: A0A0E4CZB2_9BACL 
ID   A0A0E4CZB2_9BACL        Unreviewed;       930 AA.
AC   A0A0E4CZB2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 18.
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=PRIO_6030 {ECO:0000313|EMBL:CQR58399.1};
OS   Paenibacillus riograndensis SBR5.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR58399.1, ECO:0000313|Proteomes:UP000033163};
RN   [1] {ECO:0000313|EMBL:CQR58399.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBR5 {ECO:0000313|EMBL:CQR58399.1};
RA   Wibberg Daniel;
RL   Submitted (MAR-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, ECO:0000256|SAAS:SAAS00730191}.
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; LN831776; CQR58399.1; -; Genomic_DNA.
DR   RefSeq; WP_020426197.1; NZ_LN831776.1.
DR   EnsemblBacteria; CQR58399; CQR58399; PRIO_6030.
DR   KEGG; pri:PRIO_6030; -.
DR   PATRIC; fig|1073571.4.peg.6469; -.
DR   KO; K01595; -.
DR   Proteomes; UP000033163; Chromosome I.
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:UP000033163};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CQR58399.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CQR58399.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033163}.
FT   ACT_SITE    153    153       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    587    587       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   930 AA;  106677 MW;  F0F4B3DC3BBB4919 CRC64;
     MTELTTAVSK SNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSLFLP
     ELHNEFKELI NSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
     ESAIQELRER DFSHEDVHEI MNGLSLELVM TAHPTEAMRR AILDIHKRIS DDVMGLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFQ VLPDVYQELE
     RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTAAVTL QTLRLQRKLA IREYQRIMRE
     LMQYLSFSTS IVKVTPELLQ SIESDRDIIQ LDKAKSWHND NEPYRIKLAY MIAKTQNVMD
     DEKKGTPERY ASPEQFIDDL NVIDRSLRHH YADYVADTYI KKLIRQVELF GFHTATLDVR
     QHSQEHENAM TEILAKMNVT QDYAKLQENE KIGLLEKLLN DPRPLTSPYQ TYSESTEECL
     AVYRAIFTAQ EEYGKQCITS YLISMAEAAS DILEVMVFSK EVGLFRKDND GTVVCTLQAV
     PLFETIDDLH NAPQIMRTLL NLPIYRDAVR AMNDLQEIML GYSDSNKDGG VVTANYELRV
     ALKEITTTAD EFGIKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
     RYSMQGIAYR SLEQATSALI TAAINARSPQ ADLYDPKWEE IVARISEVSL SKYQDLIFRD
     PDFLNYFKES TPLPEVGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSFYDDK EENLKIMQHM YEKFSFFTTL IDTLQMAIAK ADLIIAKEYA GMGKNEEARQ
     RIFGQIEAEF KLTSELILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLSELRA
     LREAEGDDAE LLREVLLTIN GIAAGLRNTG
//
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