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Database: UniProt/TrEMBL
Entry: B9L0J1_THERP
LinkDB: B9L0J1_THERP
Original site: B9L0J1_THERP 
ID   B9L0J1_THERP            Unreviewed;       928 AA.
AC   B9L0J1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   28-MAR-2018, entry version 71.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:ACM05187.1};
GN   OrderedLocusNames=trd_1060 {ECO:0000313|EMBL:ACM05187.1};
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM05187.1, ECO:0000313|Proteomes:UP000000447};
RN   [1] {ECO:0000313|EMBL:ACM05187.1, ECO:0000313|Proteomes:UP000000447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2
RC   {ECO:0000313|Proteomes:UP000000447};
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E.,
RA   Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R.,
RA   Ward N.L., Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; CP001275; ACM05187.1; -; Genomic_DNA.
DR   STRING; 309801.trd_1060; -.
DR   EnsemblBacteria; ACM05187; ACM05187; trd_1060.
DR   KEGG; tro:trd_1060; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000000447; 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; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 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:SAAS00946757}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000447};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACM05187.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACM05187.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000447}.
FT   COILED      109    129       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    159    159       {ECO:0000256|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    589    589       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   928 AA;  104584 MW;  D155B6CE8F37BF7D CRC64;
     MAGGRALDDE RSAKALRAEP IEGLRNEVNL LGALLGDVLR EQGGTELFDL VEWARLQSIT
     GRTVGNMSDA FRGLLARLEE ASDEEIFGLV RAFGIFFHLI NLAEQHHRVR TLRQRERQER
     ALHESLEEAF LTLRDRGVEP DRVKELLDDL LLFPVLTAHP SETRRRTVLQ RLAALGQLIQ
     QLDDTRLSPR ERDWLFDRLR EEITLLWQTA ETRLARPTPL DEVRSTIAIL AGPIYDVVPF
     FRRALRRAIL RAYPELTSEA LWNRLPIRIG SWVGGDRDGN PAVTAAVTEA TARLMREAIL
     RRYLEEVVDL RRALSVSARL RGASDELMAT IDQERERLGF APVRAWADEP YRRMLGLIEE
     RLRRTERGEQ GGYAGPEEFA THLKVMADSL RQHEGHWIAD GRLADLIARV DVFGFHLAEL
     EIRQDAARYR EALAELFALV GCAGYEAMPS DEREHLVLTR LEQGVFGLPR GALSPDTREV
     LATFDAIGRI QRLSGERACH TVIVSMTREP ADVLGTVVLA REAGLIDFAT DGAVRHCRID
     VVPLFEQIAE LDRCDQILAR LLANPIYRTV VRLRGNQQEV MLGYSDSNKD GGYVSSNWRI
     YRAQERLAEV ARQFGAQLRL FYGRGGAIGR GGGPMGRAIR ARPAAARRPV LKTTEQGEVI
     FARYSDPAIA LRHWEQMTHA SIGSLGSDPD PSMPESWYRM MEQLATWSQE AYERLVKDEP
     TFVRFFTSAT PFPELASLNL ASRPVARRGS PESGLCFADL RAIPWVFSWT QTRVNLPGWY
     GLGTALERAL AAGEESTLRE MYYRWPFFEM LLDNAQISLA TADMLIAECY ATLAGDDGWI
     AERIAEEYQR AVRTILAVTG QCELLERSPI LARLVRLRNP YVDVLHACQI VLLRRYRAGA
     GKGERQSRLL DAIHHSINAI AAGLQTTG
//
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