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Database: UniProt/TrEMBL
Entry: A0A089J095_PAEDU
LinkDB: A0A089J095_PAEDU
Original site: A0A089J095_PAEDU 
ID   A0A089J095_PAEDU        Unreviewed;       930 AA.
AC   A0A089J095;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 20.
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=PDUR_24035 {ECO:0000313|EMBL:AIQ14614.1};
OS   Paenibacillus durus (Paenibacillus azotofixans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=44251 {ECO:0000313|EMBL:AIQ14614.1, ECO:0000313|Proteomes:UP000029409};
RN   [1] {ECO:0000313|EMBL:AIQ14614.1, ECO:0000313|Proteomes:UP000029409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1735 {ECO:0000313|EMBL:AIQ14614.1,
RC   ECO:0000313|Proteomes:UP000029409};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009288; AIQ14614.1; -; Genomic_DNA.
DR   RefSeq; WP_042209649.1; NZ_CP009288.1.
DR   EnsemblBacteria; AIQ14614; AIQ14614; PDUR_24035.
DR   KEGG; pdu:PDUR_24035; -.
DR   KO; K01595; -.
DR   Proteomes; UP000029409; 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:UP000029409};
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:AIQ14614.1}.
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;  106739 MW;  9D3344B990050A12 CRC64;
     MTELTTTASK VNSNNLLRRD VRFLGNILGE VLVHQGGNEL LEIVEKIRET SKSLRSVCLP
     ELHSEFKELI DSLDPENRHQ VIRAFAIYFQ LVNIAEQNHR IRRKRDYERS AGETVQPGSI
     ESAIQELRER DFSPKEVWEI VNGLSLELVM TAHPTEAMRR AILDIHKRIA DDVTGLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETIFH VLPDVYQELE
     RCLSKYYPGQ NWHVPTYLRF GSWIGGDRDG NPSVTSSVTL QTLKMQRILA VREYQRIMRE
     LMQYLSFNTS IVKVTPELLE SIAKDRAAIK LDRFDAWRND NEPYRIKLSY MISKTQNVLD
     EEKRGTSEYY TSPAELIQDL NIIDRSLRHH FADYVADTYI KKLIRQMELF GFHTATLDIR
     QHSKEHENAM TEILAKMDIT PDYSKLSEQE KIELLEKLLN DPRPLTSPYQ EYSEGTEECL
     EVYRTVYKAQ AEYGKQCITS YLISMAEAAS DILEVMVFAK EVGLFRRDAD GTVVCTLQAV
     PLFETIDDLH EAPDIMRTIF NMPIYRQAVA AMSDLQEIML GYSDSNKDGG VVTANWELRV
     ALKGLTAMAD EYGVKLKFFH GRGGALGRGG MPLNRSILAQ PASTIGGGIK ITEQGEVLSS
     RYAMKGIAYR SLEQATSALV IAAINARTPH SDLYDSKWEE ICREISEVSL NKYQDLIFRD
     PDFLSFFKES TPLPEIGELN IGSRPSKRKN SDRFEDLRAI PWVFAWTQSR FLLPAWYAAG
     TGLQSFYQGK EENLKILQHM YGNFSFFTSL IDTLQMAIAK ADLTIAREYA EMGKNTEANQ
     RIYGQIEEEF RLTSDLILKI TGQQDILDNV PVIQESIRLR NPYVDPLSYL QVQLLTELRA
     LRDKDQDDPE LLREVLLTIN GIAAGLRNTG
//
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