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Database: UniProt/TrEMBL
Entry: A0A1R0YQR1_9BACL
LinkDB: A0A1R0YQR1_9BACL
Original site: A0A1R0YQR1_9BACL 
ID   A0A1R0YQR1_9BACL        Unreviewed;       930 AA.
AC   A0A1R0YQR1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
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=BSK60_29760 {ECO:0000313|EMBL:OME08203.1}, BSO21_15215
GN   {ECO:0000313|EMBL:OMD33385.1};
OS   Paenibacillus odorifer.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=189426 {ECO:0000313|EMBL:OME08203.1, ECO:0000313|Proteomes:UP000187446};
RN   [1] {ECO:0000313|EMBL:OME08203.1, ECO:0000313|Proteomes:UP000187446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F4-0242 {ECO:0000313|EMBL:OME08203.1,
RC   ECO:0000313|Proteomes:UP000187446};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OMD33385.1, ECO:0000313|Proteomes:UP000187158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0433 {ECO:0000313|EMBL:OMD33385.1,
RC   ECO:0000313|Proteomes:UP000187158};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OME08203.1}.
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DR   EMBL; MPVP01000089; OMD33385.1; -; Genomic_DNA.
DR   EMBL; MPTN01000045; OME08203.1; -; Genomic_DNA.
DR   RefSeq; WP_038573414.1; NZ_MPVP01000089.1.
DR   GeneID; 31573824; -.
DR   KEGG; pod:PODO_27340; -.
DR   KO; K01595; -.
DR   Proteomes; UP000187158; Unassembled WGS sequence.
DR   Proteomes; UP000187446; Unassembled WGS sequence.
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:UP000187158,
KW   ECO:0000313|Proteomes:UP000187446};
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:OME08203.1}.
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;  106915 MW;  FDF66C33ADC2C8F6 CRC64;
     MTELTTTVSK SNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSLFLP
     ELHSEFKELI NSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
     ESAIQELRER DFSHEEVNEI IEGLSLELVM TAHPTEAMRR AILDIHKRIS DDVMGLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFH VLPDVYQELE
     RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTSTVTA QTLRMQRKLA IREYQRIMRE
     LMKYLSFSTS IVKVTPELVE SIEADRQIIN LGKMEEWRND NEPYRIKLSY MISKTQNVLD
     DEKKDTPERY ATPEEFIDDL NVIDRSLRHH YADYVADTYI KKLIRQVELF GFHTATLDVR
     QHSQEHENAM TEILAKMNIS PDYSKLTEIE KIDLLEKLLN DPRPLTSSYQ TYTESTEECL
     AVYRTIFASQ EEYGKQCITS YLISMAEAAS DILEVMVFAK EVGLFRKDND GTVVCTLQAV
     PLFETIDDLH EAPQIMNTLL NMPIYRDAVR AMNDLQEIML GYSDSNKDGG VVTANWELRV
     ALKEITATAD KFGIKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
     RYSMQGIAYR SLEQATSALV TAAISARVPQ ADLYEEKWEE IVARISEVSL NKYQDLIFRD
     PDFLTYFKES TPLPEVGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSFYEGK EENLKIMQHM YENFSFFTTL IDTLQMAISK ADLIIAKEYA SMGKNEEARQ
     RIFGQIEDEF NLTSELILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLSELRA
     LREIDGDDSE LLREVLLTIN GIAAGLRNTG
//
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