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Database: UniProt/TrEMBL
Entry: A0A127K5R2_9RHOO
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Original site: A0A127K5R2_9RHOO 
ID   A0A127K5R2_9RHOO        Unreviewed;       916 AA.
AC   A0A127K5R2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-NOV-2017, entry version 13.
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   ORFNames=AC731_010250 {ECO:0000313|EMBL:AMO37300.1};
OS   Thauera humireducens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Thauera.
OX   NCBI_TaxID=1134435 {ECO:0000313|EMBL:AMO37300.1, ECO:0000313|Proteomes:UP000036902};
RN   [1] {ECO:0000313|EMBL:AMO37300.1, ECO:0000313|Proteomes:UP000036902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SgZ-1 {ECO:0000313|EMBL:AMO37300.1,
RC   ECO:0000313|Proteomes:UP000036902};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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; CP014646; AMO37300.1; -; Genomic_DNA.
DR   RefSeq; WP_048705819.1; NZ_CP014646.1.
DR   EnsemblBacteria; AMO37300; AMO37300; AC731_010250.
DR   KEGG; thu:AC731_010250; -.
DR   KO; K01595; -.
DR   Proteomes; UP000036902; 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:UP000036902};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AMO37300.1}.
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   916 AA;  101353 MW;  D9B054BC0AD55531 CRC64;
     MTQDKDAPLR EDIRLLGRLL GDTVRDQQGA AAFELIERIR QNSVRFRRDD DIAARRELED
     MLDALSRDQT IQVVRAFSYF SHLANIAEDQ HHIRRSRAHL IAGSAPREGS LAHALEAALA
     SGTTDAAGLV EFFDTARVSP VLTAHPTEVQ RKSILNCETV IARLLDERDR MQLTPEESEA
     NLEALRRAVL TLWQTRILRT AKLSVIDEVN NGLSYFDTTF LRELPRLYAS LEDRLATAAP
     GLTGTELANF LQVGSWIGGD RDGNPFVTAE VLDKALAMHA AVALEYYLNE LHTLGSQLSM
     SHGFVSASDA LLALAEHSGD HSPHRSDEPY RRAVSGLYAR LAATYRELLG HEPARHAVAR
     AEPYADAAAL SEDLDTLHRS LVANGSAALS RGRLRQLRRA VKVFGFHLAP IDLRQNSDVH
     ERVVAELLET ARPGTDYRAQ DETGRCALLL EELATARPLA SPHVRYSDET EGELAIFRTA
     RRAHQRYGRA AIRHCIISKT DDVSDLLELA VLLKEAGLLR PLENALDVDI VPLFETIGDL
     ENAAGVMERL FSLPIYRNLL AARGQTQEVM LGYSDSNKDG GFLTSGWALY KAEGELVATF
     ARHGVRLRLF HGRGGSVGRG GGPSYQAILA QPDGAVQGQI RLTEQGEVIG AKYGNPEVGR
     RNLEVLVAAT LETSLRPAGA EPTPPAFMDA MQALSDAAFT AYRGLVYDTE GFERYFWEST
     VISEIAALNI GSRPASRKKS TAIEDLRAIP WVFSWSQCRV MLPGWYGFGS AVQAFLARHP
     QDGLALLQRM HREWSFFATL LSNMDMVLAK SDLAIASRYA DLVKDVALRE AIFGRIRAEH
     QATVEALLQI TGQRELLEAN PLLKRSIRNR FPYLDPLNHV QVELLRRHRE HGDDPRIRNG
     IHISINGIAA GLRNSG
//
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