ID   D6Y5T0_THEBD            Unreviewed;       890 AA.
AC   D6Y5T0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
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|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Tbis_0701 {ECO:0000313|EMBL:ADG87426.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS   10125 / KCTC 9307 / NBRC 14880 / R51).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG87426.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG87426.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC   NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP001874; ADG87426.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6Y5T0; -.
DR   STRING; 469371.Tbis_0701; -.
DR   KEGG; tbi:Tbis_0701; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000006640; 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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ADG87426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006640}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        552
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   890 AA;  97926 MW;  F80DB6E41451E8FE CRC64;
     MAAIAHTAAN GAPEPGSEGV SERLDAVAEM PDELRADVRL LGELLGQVIA EQGGPDLLAD
     VERLRKAVIA AKRGETTADE IAAMVAEWPI DRAVQIARAF TCYFHLVNLA EEHHRIRSLR
     QRDQGGVPLR ESIAEAVERL RDDERLGDLI ENLEFHPVLT AHPTEARRRA IVTAIQRISA
     QLGVYRTAAG ASEREEAKRR LIEEIDILWR TAQLRPTKLD PLDEVRTAMA VFDETLFRVV
     PKIYRTLDAA LAPGTGTREP RARAFIRFGS WIGGDRDGNP YVTARVTREA IQIQAEHVLI
     ALENATSRIG RALTVANLFT PPSAELSAAI AQAEGDHPDL MSELAKRSPR EPHRQWLLFV
     AARIAATRRR DLDLAYRSPD ELLADLRLVQ RSLRDAGAVR QAYGELQHLI WQVETFGFHL
     AELEIRQHSE VHAVALKEIA SGSLSERTEE VLATFRTIAW IQERFGVAAC SRYIVSFTRS
     AADIAAVYEL ARHALGDRAP VLDVVPLFES GDDLEHAPEV LDGMLRLEPV RERLAANGRR
     LEVMLGYSDS AKEIGPAAAT LRLYDAQAAL AEWARANDIR LTLFHGRGGA LGRGGGPANR
     AVLAQAPGSV AGRFKVTEQG EVIFARYGHA EIARRHIEQV TNAVLLASTP AVESKAAEAA
     ARFRELAELV AAASERAYRA LVEAPGFPEW FALVSPLEEI GRLRIGSRPP RRGLGAPRSL
     DDLRAIPWVF AWAQTRVNLP GWYGLGSGLA AAEASRGMDE LRAAYREWPL FASMMDNAEM
     SLAKTDRAIA ARYLALGGRE DFAEQVLGEY DLTRRLVLEV TGHRRLLENR RVLSRAVQLR
     NPYVDALSHL QLRALAALRA GGLSETERER LSTLLLLSVN GVAAGLQNTG
//