ID   H6RQV8_BLASD            Unreviewed;       939 AA.
AC   H6RQV8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   ECO:0000313|EMBL:CCG01635.1};
GN   OrderedLocusNames=BLASA_0679 {ECO:0000313|EMBL:CCG01635.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG01635.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG01635.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG01635.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, 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; FO117623; CCG01635.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6RQV8; -.
DR   STRING; 1146883.BLASA_0679; -.
DR   KEGG; bsd:BLASA_0679; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000007517; 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; IPR033129; PEPCASE_His_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; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 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:CCG01635.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   939 AA;  102754 MW;  2E2C51ADC973D864 CRC64;
     MSEATVDVAD LRHHGSAGPG GRADDEPLRE DIRLLGRILG EVIGEHAGPD VLELVESTRL
     EAFGVRRSEV DRVALAARLD GLDVRSANHI IRAFSHFSVL ANLAEDIHHE RRRRHHRRAG
     SPPQRGSLAA TFELLDRAGL SEDTVARELA GALVCPVVTA HPTEVRRKTV FQVQRQIAEL
     IRQRDRAGGG DVDDEWSARM SRSVLTLWQT ALLRLSRLRL EDEIDEALRY YELSLFDVVP
     AINADLRRAV EERWPGAGVL RRPMLLPGSW IGGDRDGNPF VTADALRRAT TRQAETALGH
     HLAELAELRS ELSMSDRLIT STPELYALAD ASGDDSPFRA DEPYRRALTG ITARLAATAL
     RVLGTVPGGR VAGPDVVAYA VPDELRADLD VVDASLRSHG AGALADDRLR RLREAVEVFG
     FHLCGLDLRQ NSAVHEEVVA ELLAWAGVCE DYAALDEVAR VELLAGELTL RRPLVRPDAQ
     LSEGARKELD VLLAAAGQVA LLGPRTIPNY VVSMCESVSD VLEVAVLLKE VGLLDPGGVD
     GPTCPVGISP LFETIGDLQA AASTLGAVLD QPLYRSLLGN RGDVQEVMLG YSDSNKDGGY
     LAANWALYRA ELDLVEVARR EGIRLRLFHG RGGTVGRGGG PSYEAVRAQP PGAVAGALRI
     TEQGEVIAAK YADPDLARRN LEALVAATLE STLLDVEGLG QDADEAYALL DDLAARAQLA
     YRELVHETPG FVEWFRAATP IGELAELNIG SRPPSRKAGD SIADLRAIPW VFSWSQTRIM
     LPGWYGTGSA LESFVDGSPE RLERLRDLHR RWPFFRTILS NMGMVLAKTD LGLAARYAGL
     VPDEELRARV FDRIREEHER TCRMTRAITG EDDLLADNPS LARSIRNRFP YLEPLHHLQV
     EMLRRRRSAV SGEDPDDELT SRNIQLTING IATALRNSG
//