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Database: UniProt/TrEMBL
Entry: Q47LT5_THEFY
LinkDB: Q47LT5_THEFY
Original site: Q47LT5_THEFY 
ID   Q47LT5_THEFY            Unreviewed;       875 AA.
AC   Q47LT5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-SEP-2017, entry version 86.
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=Tfu_2554 {ECO:0000313|EMBL:AAZ56587.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56587.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ56587.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q47LT5; -.
DR   STRING; 269800.Tfu_2554; -.
DR   EnsemblBacteria; AAZ56587; AAZ56587; Tfu_2554.
DR   KEGG; tfu:Tfu_2554; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000000434; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:UP000000434};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AAZ56587.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AAZ56587.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   ACT_SITE    145    145       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    539    539       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   875 AA;  97467 MW;  F98D315840D149B0 CRC64;
     MTRDSARQEM PDQLRRDVRL LGEMLGTVLA ESGGQDLLDD VERLRRAVIG AREGTVEGKE
     ITELVASWPL ERAKQVARAF TVYFHLVNLA EEHHRMRALR ERDDAATPQR ESLAAAVHSI
     REDAGPERLR ELIAGMEFHP VLTAHPTEAR RRAVSTAIQR ISAQLERLHA AHPGSGAEAE
     ARRRLLEEID LLWRTSQLRY TKMDPLDEVR TAMAAFDETI FTVIPEVYRS LDRALDPEGC
     GRRPALAKAF VRYGSWIGGD RDGNPFVTHE VTREAITIQS EHVLRALENA CERIGRTHTE
     YTGLTPPSAE LRAALSSARA AYPRLMQEII KRSPNEPHRQ LLLLAAERLR ATRLRNADLG
     YPNPEAFLAD LRTVQESLAA AGAVRQAYGE LQNLIWQAET FGFHLAELEI RQHSAVHAAA
     LKEIRAGGEL SERTEEVLAT LRVVAWIQER FGVEACRRYI VSFTQSADDI AAVYELAEHA
     MPPGKAPILD VIPLFETGAD LDAAPQVLDG MLRLPAVQRR LEQTGRRMEV MLGYSDSAKD
     VGPVSATLRL YDAQARLAEW AREHDIKLTL FHGRGGALGR GGGPANRAVL AQAPGSVDGR
     FKVTEQGEVI FARYGQRAIA HRHIEQVGHA VLMASTESVQ RRAAEAAARF RGMADRIAEA
     AHAAYRALVD TEGFAEWFSR VSPLEELSEL RLGSRPARRS AARGLDDLRA IPWVFAWTQT
     RVNLPGWYGL GSGLAAVDDL EALHTAYKEW PLFASLLDNA EMSLAKTDRV IAERYLALGG
     RPELTEQVLA EYDRTRELVL KVTRHTRLLE NRRVLSRAVD LRNPYVDALS HLQLRALEAL
     RTGEADRLSE EDRNHLERLL LLSVNGVAAG LQNTG
//
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