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Database: UniProt/TrEMBL
Entry: A0A0F7KBW6_9PROT
LinkDB: A0A0F7KBW6_9PROT
Original site: A0A0F7KBW6_9PROT 
ID   A0A0F7KBW6_9PROT        Unreviewed;       932 AA.
AC   A0A0F7KBW6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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=AAW31_09190 {ECO:0000313|EMBL:AKH37955.1};
OS   Nitrosomonas communis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH37955.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-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; CP011451; AKH37955.1; -; Genomic_DNA.
DR   RefSeq; WP_046850023.1; NZ_CP011451.1.
DR   EnsemblBacteria; AKH37955; AKH37955; AAW31_09190.
DR   KEGG; nco:AAW31_09190; -.
DR   PATRIC; fig|44574.3.peg.2242; -.
DR   KO; K01595; -.
DR   Proteomes; UP000034156; 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:UP000034156};
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:AKH37955.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034156}.
FT   ACT_SITE    158    158       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    591    591       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   932 AA;  105814 MW;  AC4D5BE4E9DA8528 CRC64;
     MSSDAGVSVY SDNNMSEEKD KPLREDIRML GRMLGDTLRE QEGEATFELV ETIRQTAVRF
     RREQDPKARQ ELDMILNRLS NKATIAVVRA FSYFSLLSNI AEDLHHNRRR RAHLRQGSSP
     QPGSVTLALE RVLASGIDNA SLDNFFAQAM ISPVLTAHPT EVQRRSILDC QLTIQRLLQE
     RDRIQLTPNE LRHNEEALRA AIQILWQTRM LRSVRLTVHD EIENGLIYYT YTFLSQVPYI
     YAKIEDLLER HKGKEAPHVA SFLRIGSWIG GDRDGNPFVT HQVMLHAAER QATLVFDFYM
     DEVSKIGRTM SLAERLIHVS EELEQLAAAS PDIPASRIDE PYRRAFLGIY ARLAATSRQR
     GLAAMPREPV NPTEPYADSA EFIHDLDVVI DSLKQHRSDW LARGALRNLR RAVDVFGFHL
     ASLDMRQHSK VHEQVVAELF ARGTRRDNYL ELSASERMKW LLAEISSLRL LHSPYLTYSE
     PTQSELRILQ MAAEIQRRFG HAALPNYIIS MTTGVINILE VALLLKEAGL LRAGEKPQLG
     LNIIPLFETI EDLRSCSTVM DELFSLPYYR KLLDSRGNVQ EVMLGYSDSN KDGGFLTSNW
     EIYKAEIELT KIFAKHQVEL RLFHGRGGTV GRGGGPSYQG IMAQPPSSVN GQIRLTEQGE
     VVASKYTDPE IGRRNLETLV AATIEATLLS HDAIQENAAH YYHVMETLSS SAFAVYRNLV
     YETPGFKQFF QESTPIREIA GLHIGSRPSS RKPSDRIEDL RAIPWVFSWS LNRTMLPGWY
     GFGSAVEAFV QQAQGEETGL QLLQEMYQKW PFLQTLLSNM DMVLAKTDMG IASRYAELVT
     DATLRNQIFG RIQAEWERSV KWLFAITGHT ALLQENPTLA RSIRIRTPYI DPLNHLQIEL
     LRRYRAGDDV EQVHRSIHLT INGVAAGLRN SG
//
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