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Database: UniProt/TrEMBL
Entry: C4ZNN2_THASP
LinkDB: C4ZNN2_THASP
Original site: C4ZNN2_THASP 
ID   C4ZNN2_THASP            Unreviewed;       920 AA.
AC   C4ZNN2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   22-NOV-2017, entry version 64.
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=Tmz1t_1436 {ECO:0000313|EMBL:ACK54195.1};
OS   Thauera sp. (strain MZ1T).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Thauera.
OX   NCBI_TaxID=85643 {ECO:0000313|EMBL:ACK54195.1, ECO:0000313|Proteomes:UP000002186};
RN   [1] {ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) 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: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; CP001281; ACK54195.1; -; Genomic_DNA.
DR   RefSeq; WP_004308693.1; NC_011662.2.
DR   ProteinModelPortal; C4ZNN2; -.
DR   STRING; 85643.Tmz1t_1436; -.
DR   EnsemblBacteria; ACK54195; ACK54195; Tmz1t_1436.
DR   KEGG; tmz:Tmz1t_1436; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002186; 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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002186};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ACK54195.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ACK54195.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002186}.
FT   ACT_SITE    145    145       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    578    578       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   920 AA;  100892 MW;  6381D58AD7C598E2 CRC64;
     MNQDKDAPLR DDIRLLGRLL GDTVRDQQGE AAFGLIERIR QNSVRFRRDD DIAARRELED
     ILDALSREQT IQVVRAFSYF SHLANIAEDQ HHIRRSRAHL IAGSAPREGS LAHALERALD
     SGAADPAALA GFFDGALVSP VLTAHPTEVQ RKSILNCETV IARLLDARDR MQLTPEEAEA
     NDEALRRAVL TLWQTRMLRT AKLSVIDEVN NGLSYFETTF LRELPRLYAS LEDRLAAADR
     ALGTPELAAF VQVGSWIGGD RDGNPFVTAE VLERALAMQC AVALGHYLDE LHILGSQLSL
     GIGLVSASDA LLALAEASPD HSPHRSDEPY RRAISGIYAR LAATYRSLLG HDPLRHAVAA
     AQPYPSAAAL AEDLEVLHRS LAANGSGALT RGRLRHLRRA VKVFGFHLAP LDLRQNSDVH
     ERTVAELLER ACPGTAYASL DEDARCALLL EELATARPLA SPHVRYTDET EGELAIFRAA
     RQAHLRYGTA AIRNCIISKT DDVSDLLELA VLLKEAGLLR PLENALDVNI VPLFETIGDL
     ENAAGVMARI FSIPAYRGLL EARDHTQEVM LGYSDSNKDG GFLTSGWALY KAEGELVETF
     ARHGVRLRLF HGRGGSVGRG GGPSYQAILA QPEGAVQGQI RLTEQGEVIG AKYGNPEVGR
     RNLEVLVAAT LESSLRPASA SPTPPAFLDA MQALSDAAFA AYRGLVYETE GFERYFWEST
     VISEIAALNI GSRPASRKKS TAIEDLRAIP WVFSWSQCRV MLPGWYGFGS AVRDFLTANP
     DDGLALLQRM NMEWPFFQTL LSNMDMVLSK TDLAIASRYA ELVKDAALRD TIFGRIRAEH
     QATVGAVLRI TGQSELLDAN PLLKRSIRNR FPYLDPLNHV QVELLRRHRD AAEAGGIDER
     IRLGIHISIN GIAAGLRNSG
//
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