ID K7R4S3_THEOS Unreviewed; 858 AA.
AC K7R4S3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, 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 ORFNames=Theos_0883 {ECO:0000313|EMBL:AFV75939.1};
OS Thermus oshimai JL-2.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=751945 {ECO:0000313|EMBL:AFV75939.1, ECO:0000313|Proteomes:UP000000211};
RN [1] {ECO:0000313|EMBL:AFV75939.1, ECO:0000313|Proteomes:UP000000211}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JL-2 {ECO:0000313|EMBL:AFV75939.1,
RC ECO:0000313|Proteomes:UP000000211};
RX PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA Hedlund B.P.;
RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL Genome Announc. 1:E00106-E00112(2013).
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; CP003249; AFV75939.1; -; Genomic_DNA.
DR RefSeq; WP_016329130.1; NC_019386.1.
DR AlphaFoldDB; K7R4S3; -.
DR STRING; 751945.Theos_0883; -.
DR KEGG; tos:Theos_0883; -.
DR PATRIC; fig|751945.3.peg.875; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_0; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000000211; 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; 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:AFV75939.1}.
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 531
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 858 AA; 95332 MW; 7C48202D5A43F557 CRC64;
MREDPFSLLK EEVDLLGRLL GEAIGRVSGE RFFALVEEVR LLSKARRQGD EGAGEALLAK
AGALSVAEAE ALVRAFTHYF HLVNLAEERH RVRVNRLRAE AETPEAPRPE GPLALAQALK
ARGLSLEEAE AHLNRLELLL TFTAHPTETR RRTLRHHLER IQEVLERGDR EELKARVALL
YATEEVRKAR PSVEDEIKGG LYYLPTTLWK AVPLLLERLE AAFERVYGKR PRLKSPVRFR
SWIGGDRDGN PFVTPEVTAF AAAYARRVAK ERYLAELEAL VRDLSLSEAR LPAPRAVREG
GEGVERFPGE PYRRYFAALY GKLEGEALSE EDFARALLQA ERGLEEAGLG EVARVFLRPL
SARLSAFGLA LAPLDLREES GKLLEAAAEL LRLGGVHPDF LGLPEEAQEA LLTEELKTPR
PLLPVGQAPE GEALRVALGA LRAWRDRGAH VVSMAHGPRD VLAVFLLARE VGDYRPGKPL
PYDVAPLFET LEDLRRAPQV LRRLLQNPVF LAHARGRGGV EVMIGYSDSN KDAGFLAANL
ALYQAQEALA AVGREAGLRV HFFHGRGTST ARGGGPAGRA IASLPPRSVG HRLRLTEQGE
ALADRYGHVE LAVRHLEQLL YHFALAALAE GGDPRPSWLE ALEEAAALSV ERYRALLQAE
GFFPFFEHLT PIREIGELPI ASRPVYRHGR VRDIRDLRAI PWVMAWTQVR LLLPGWYGLS
ALEGLPLSLL QEMYRGWPFF ATTLESAAMA LAKADLGVAR LYLRLVPEPL RPLFDRIAEE
YRKTVALLEA VFQAPLLHNQ KTLERQIALR NPYVDPINLL QVELLRRYRA PGGAEDEALK
KALLLSILGV AAGLRNAG
//
