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Database: UniProt/TrEMBL
Entry: F8GFD3_NITSI
LinkDB: F8GFD3_NITSI
Original site: F8GFD3_NITSI 
ID   F8GFD3_NITSI            Unreviewed;       931 AA.
AC   F8GFD3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-SEP-2017, entry version 37.
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   OrderedLocusNames=Nit79A3_0126 {ECO:0000313|EMBL:AEJ00033.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ00033.1, ECO:0000313|Proteomes:UP000000501};
RN   [1] {ECO:0000313|EMBL:AEJ00033.1, ECO:0000313|Proteomes:UP000000501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ00033.1,
RC   ECO:0000313|Proteomes:UP000000501};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A.,
RA   Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D.,
RA   Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) 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; CP002876; AEJ00033.1; -; Genomic_DNA.
DR   RefSeq; WP_013964336.1; NC_015731.1.
DR   STRING; 261292.Nit79A3_0126; -.
DR   EnsemblBacteria; AEJ00033; AEJ00033; Nit79A3_0126.
DR   KEGG; nii:Nit79A3_0126; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000000501; 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:UP000000501};
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:AEJ00033.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000501}.
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;  105735 MW;  A5126BC008B0C341 CRC64;
     MNAADSENNV ANNKLVDDKD LPLREDIRFL GRMLGDTLRE QDGDGAFELV ENIRQTAIRF
     HRDQDLKARD ELDALLNRLS DKDSLPVVRA FSYFSLLSNI AEDVHHNRRR RAHLRAGSPP
     QAGSVTLALE RVLESRKDIT VLAEFFNKAM ISPVLTAHPT EVQRRSILDC QLTIERLLKE
     RARTELTPNE LRHNEEGLRA TIQILWQTRM LRPTRLSVYD EIENGLAYYS YTFLTEIPYI
     YAKIEDLLER RLVKDVPYVT SFLRIGSWIG GDRDGNPFVT HDVMLRAVER QSSVALDFYI
     DAVQKIGRSM SLTEQLVQVS DEVKQLAATA PDIPNRSDEP YRRIFLSIAA RLVATAHQLG
     HQVTQYTPGE ARAPYASSTE FLHDLNAIIH SLKQHKSSWI ARGSLRNLCR AVDVFGFHLA
     PLDMRQHSKI HEQVVGELFE HSTGRKGYAQ LSEKDRIEWL LKEISLPRSI LASYADFSEL
     AQSELRILQC AAEIHRRFGR VAMSNYIISM TTDIINVLEV AFLLQQVGLL QAGENPQLFL
     NIIPLFETIS DLRSCSNIMD QLFSLPYYRK LLSSRGNVQE VMLGYSDSNK DGGFITSNWE
     IYKAEIELTK VFAKHQVELR LFHGRGGTVG RGGGPSYQSI LAQPPGSVNG QIRVTEQGEV
     ISSKYAEPEI GRRNLETLVA ATLEATLLSH DSLGANADRY YPAMEMLASA SFAAYRDLVY
     ETPGFKQFFL ESTPIREMAG LHIGSRPPSR KNSDAIEDLR AIPWVFSWSL SRMMLPGWYG
     FGHAVEAFVN REDQPGQGLQ LLQEMYQNWP FMQTLLSNMD MVLTKTDMGI ASRYAELVED
     VALREQIFGR IKDEWARSQK WLFAVTGHTE LLQDNPTLAR SIRNRTPYID PLNHLQVELL
     RRYRSGEDSE EVKRSIHLTI NGVTAGLRNS G
//
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