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Database: UniProt/TrEMBL
Entry: A0A0S3AH84_9PROT
LinkDB: A0A0S3AH84_9PROT
Original site: A0A0S3AH84_9PROT 
ID   A0A0S3AH84_9PROT        Unreviewed;       931 AA.
AC   A0A0S3AH84;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=ATY38_03580 {ECO:0000313|EMBL:ALQ50395.1};
OS   Nitrosomonas ureae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44577 {ECO:0000313|EMBL:ALQ50395.1, ECO:0000313|Proteomes:UP000056699};
RN   [1] {ECO:0000313|EMBL:ALQ50395.1, ECO:0000313|Proteomes:UP000056699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm10 {ECO:0000313|EMBL:ALQ50395.1,
RC   ECO:0000313|Proteomes:UP000056699};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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; CP013341; ALQ50395.1; -; Genomic_DNA.
DR   RefSeq; WP_062558091.1; NZ_FNLN01000007.1.
DR   EnsemblBacteria; ALQ50395; ALQ50395; ATY38_03580.
DR   KEGG; nur:ATY38_03580; -.
DR   KO; K01595; -.
DR   Proteomes; UP000056699; 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:UP000056699};
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:ALQ50395.1}.
FT   ACT_SITE    158    158       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    590    590       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   931 AA;  106218 MW;  BE4C7BC7B0BDF3CF CRC64;
     MNDVDSENYD INKLANDKDL PLREDIRFLG RMLGDTVREQ EGDKAFELVE NIRKIAIRFH
     REQDPTARHE LEAILKQLSD KDSLPVVRAF SYFSLLSNIA EDVHHNRRRR AHLRAGSAPQ
     AGSVTLALER VLESSSNART ILADFFKQAI VSPVLTAHPT EVQRRSILDC QLAIERLLKE
     RAWVELTPNE LRHNEENQRA TIQILWQTRM LRPTRLSVYD EIENGLAYYS YTFLSEIPYI
     YAKIEDLLER RLASDIPLVT SFLRIGSWIG GDRDGNPFVT HEVMLRAMER QSAVALEYYM
     DAVQKIGRSM SLTERLVEVS DEVKKLLATA PDIPNRSDEP YRRIFLSIGA RLVATAKKFG
     HQVLQLSTEE TKEPYADSAE FVHDLEAIIQ SLKQHKSSWV ARGALRNLRR AAEVFGFHLA
     PLDMRQHSKI HEQVVSELFE YYTGHKDYLQ LREKERIDWL LSEINRLHPL LTIPSEFSET
     TQSELRILQC AAEIHRRFGR AAMPNYIISM TTGVINILEV AYLLRQVDLL QTGENPQLHL
     NIIPLFETIS DLQSCGKIMD QLFSLPYYRK LLSSMGSVQE VMLGYSDSNK DGGFIASNWE
     IYKAEIVLTK VFAKHHVGLR LFHGRGGTVG RGGGPSYQSI LAQPPGSVNG QIRVTEQGEV
     ISSKYAEPEI GRRNLETLVA ATMEATLLGH DSIGRNADRY YPAMNKLAAI SFAAYQDLVF
     GTTGFKQFFL ESTPIREMAG LHIGSRPPSR TSSDDIEDLR AIPWVFSWSQ SRMMLPGWYG
     FGHAVETFVN QKDQNEQGLE LLQEMYQKWP FMQTLLSNMD MVLAKTDMGI ASRYAELVND
     VALREQIFAR IQEERARSEK WLFAITGNVE LLQDNPTLAR SIRNRIPYID PLNHLQVELL
     RRYRSGEDSE EVKRSIHLTI NGVTAGLRNS G
//
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