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Database: UniProt/TrEMBL
Entry: X5A5V2_9BACL
LinkDB: X5A5V2_9BACL
Original site: X5A5V2_9BACL 
ID   X5A5V2_9BACL            Unreviewed;       930 AA.
AC   X5A5V2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   22-NOV-2017, entry version 25.
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=PSAB_21425 {ECO:0000313|EMBL:AHV99174.1};
OS   Paenibacillus sabinae T27.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV99174.1, ECO:0000313|Proteomes:UP000019772};
RN   [1] {ECO:0000313|EMBL:AHV99174.1, ECO:0000313|Proteomes:UP000019772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T27 {ECO:0000313|EMBL:AHV99174.1,
RC   ECO:0000313|Proteomes:UP000019772};
RX   PubMed=24651173;
RA   Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA   Chen X., Cheng Q., Chen S., Li J.;
RT   "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing
RT   Paenibacillus spp.: Organization, Evolution and Expression of the
RT   Nitrogen Fixation Genes.";
RL   PLoS Genet. 10:E1004231-E1004231(2014).
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; CP004078; AHV99174.1; -; Genomic_DNA.
DR   RefSeq; WP_025336633.1; NZ_CP004078.1.
DR   EnsemblBacteria; AHV99174; AHV99174; PSAB_21425.
DR   KEGG; psab:PSAB_21425; -.
DR   PATRIC; fig|1268072.3.peg.4413; -.
DR   KO; K01595; -.
DR   Proteomes; UP000019772; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019772};
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:AHV99174.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019772}.
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;  107109 MW;  A59A5B783B039CC4 CRC64;
     MTELTTTAGK VNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSVFLP
     ELHSEFKELI NSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
     ESAIQELRER DFSPKEVWEI INGLSLELVM TAHPTEAMRR AILDIHKRIS DDVTGLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFH VLPDVYQELE
     RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTASVTI QTLRIQRIMA IREYQQIMRQ
     LIQYLSFSTS IVNVTPELLE SIEKDRAVVQ LERSDAWRND NEPYRIKLSY MITKTQNVLD
     DKKKGTLERY SSPEELINDL NVIDRSLRHH YADYVADTYI KKLIRQVELF GFHTATLDIR
     QHSQEHEKAM TEILAKMDIT PDYSKLTESE KIELLEKLLN DPRPLTSPYQ EYSESTEECL
     EVYRTVHAAQ AEYGKQCITS YLISMAEAAS DILEVMVFAK EVGLFRRDKD GTVVCTLQAV
     PLFETIDDLH AAPEIMRTIF NLPIYRQAVE AMSNLQEIML GYSDSNKDGG VVTANWELRV
     ALKELTAMAD SYDVKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVISS
     RYKMKGIAYR SLEQATSALV IAAINARTPH SDLYENKWED ICREISEISL TKYQDLIFRD
     PDFLSFFKES TPLPEIGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR YLLPAWYAAG
     TGLQSFYDNK EENLKILQHM YEHFSFFTSL VDTLQMALAK ADLVIAKEYS EMSKNDEARK
     RIYGQIEEEF RLTSELILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLTELRA
     LRETEQDDPD LLREVLLTIN GIAAGLRNTG
//
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