GenomeNet

Database: UniProt/TrEMBL
Entry: D1A204_THECD
LinkDB: D1A204_THECD
Original site: D1A204_THECD 
ID   D1A204_THECD            Unreviewed;       892 AA.
AC   D1A204;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   28-MAR-2018, entry version 63.
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   OrderedLocusNames=Tcur_4129 {ECO:0000313|EMBL:ACY99657.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99657.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY99657.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 /
RC   Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA   Del Rio T.G., Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Han C., Detter J.C., Rohde M., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain
RT   (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001738; ACY99657.1; -; Genomic_DNA.
DR   RefSeq; WP_012854440.1; NC_013510.1.
DR   STRING; 471852.Tcur_4129; -.
DR   EnsemblBacteria; ACY99657; ACY99657; Tcur_4129.
DR   KEGG; tcu:Tcur_4129; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; TCUR471852:G1GG3-4108-MONOMER; -.
DR   Proteomes; UP000001918; 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   PANTHER; PTHR30523; PTHR30523; 2.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001918};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACY99657.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACY99657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918}.
FT   ACT_SITE    156    156       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    552    552       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   892 AA;  98526 MW;  1B830F81F9ADB7AD CRC64;
     MRDSAAGQVP SEQRKALREE MPEPLRRDVR LLGAMLGEIL VEYGGPDLLE DVERLRHAVI
     DARQGRVSID EAAALVAGWD LERAELVARA FTVYFHLTNL AEEHHRIRAL RERDTDPAHP
     VSGSLAAAVA QIRGTGEHRL AQVLDGLEFR PVFTAHPTEA RRRAVVTAIM RISALLQDFN
     DPRKGAAERD EIRRQLREEI DLLWRTALRR HTQMDPLDEV RTAMAAFDET IFRVVPQLYR
     ALDSALDVGA SGPASGARPP RAHAYLRFGS WIGGDRDGNP YVTAQITREA VLIQSDHVLR
     ALENACTRIG RRLTVSSATT PPSAALRNAL DAARTAYPLL IAELAKRSPE EPHRQYLLYV
     AERIAATRAR HADMAYRSPE ELLADLRLVQ ESLAGAGAVR QAYGELQHLI WQTETFGFHL
     AELEIRQHSQ VHEKALAEVR AGGALSEMTE EVLDTLRVVS WIQRRFGVRA CHRYVVSFTR
     SADDIAAVYE LAESLGDHAP VLDVVPLFET GEDLDRAPSV LEGMLKLPAV QRRLAETGRR
     LEVMLGYSDS AKQLGPTSAT LRLYDAQAAL AAWAARNGIT LTLFHGRGGS LGRGGGPANR
     AILAQAPGSV NGRFKVTEQG EVIFARYGQR EIAKRHIEQV TNAIMLASTP AVEARAHEAA
     VRFRPLADRI SAAAQAAFRA LIETEGFAEW FARVSPLEEI SRLRIGSRPA RRTATRSLED
     LRAIPWVFAW TQTRVNLPGW YGLGSGLEAV LGGGDDEAGL AELQEAYRSW PLFAVMLDNA
     EMSLAKADRA IAERYLALGG RPELTERVLA EYDRTRSLVL AVTGHRRLLE NRRVLSRAVE
     LRNPYVDALS LLQLRALTAL REGVADDAER ARLEELLLLS VNGVAAGLQN TG
//
DBGET integrated database retrieval system