ID H6RQV8_BLASD Unreviewed; 939 AA.
AC H6RQV8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
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,
CC ECO:0000256|HAMAP-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 OMA; PWVFGWT; -.
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
//