ID A0A0A2WWE7_THEFI Unreviewed; 849 AA.
AC A0A0A2WWE7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 24-JAN-2024, entry version 40.
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=THFILI_07315 {ECO:0000313|EMBL:KGQ23102.2};
OS Thermus filiformis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ23102.2, ECO:0000313|Proteomes:UP000030364};
RN [1] {ECO:0000313|EMBL:KGQ23102.2, ECO:0000313|Proteomes:UP000030364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ23102.2,
RC ECO:0000313|Proteomes:UP000030364};
RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL Submitted (FEB-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ23102.2}.
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DR EMBL; JPSL02000039; KGQ23102.2; -; Genomic_DNA.
DR RefSeq; WP_038060289.1; NZ_JPSL02000039.1.
DR AlphaFoldDB; A0A0A2WWE7; -.
DR STRING; 276.THFILI_07315; -.
DR Proteomes; UP000030364; Unassembled WGS sequence.
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:KGQ23102.2}.
FT ACT_SITE 143
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 525
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 849 AA; 96023 MW; BE1A3A51C325EC03 CRC64;
MTEPFEALRR EVDLLGRLLG EAIRAVSGER FFALVEEVRL LAKARRRGEE VAEALIRRVQ
ALSPEEAEAL VRAFTHYFHL VNLAEERHRV RVNRLRAQAE TLETPRPESF LALVKALKER
GLSYEEAVAH LSSLTLLLTF TAHPTETRRR TLRHHLEALQ EELEGGEAER LLARVILLYA
TEEIRKMRPT VEDEIKGGLY YLPTTLWQAV PRAVAALEEA VERVYGKRPT LPPFVRFRSW
IGGDRDGNPH VTPEVTRFAG EYARRVAREK LLSELDRLIR DLSLSEERLP VPREVREGGE
GVDRFQGEAY RRFFLRLAQR LPEATTRDLL RQVEEARRGL RTLPAVARVH LDPLRVRLQA
FGLELAPLDL REESGRLLEA VAELFRAGGV QEDLLALSPE AQEDLFTREL LSPRPLAPVG
YEPEGEALRV ALGALRAWRD RGAHVVSMTH HPRDLLAVFL LAREVGLYRV GEGVPFDVVP
LFETLEDLDR APEVVGRLLE NPVFLAHVRA RGGLEVMIGY SDSNKDAGFL AANLALYEAQ
EAIARVGREK GVPVHFFHGR GTSTARGGGP AGRAIAGLPP GSVGRRIRLT EQGEALADRY
GHPELALRHL EQLLYHFAQA ALGEGREPLP EWRLALREAA WESVRRYRAL VEAEGFFPFF
EAFTPIRELS ELPIASRPVY RHGRVRDVRD LRAIPWVMAW TQVRLILPGW YGLSALETLP
LPLLREMYRG WPFFAATLES AAMALAKADL GVARLYLSLV PEPLHPFFHR LEAEYHRTVA
LLEEVFQAPL LHNQKTLARQ IELRNPYVDP INFVQVELLR RYRASQDEAL KRGLMLSLLG
VAAGLRNAG
//
