ID A0A0S2TBF8_9GAMM Unreviewed; 927 AA.
AC A0A0S2TBF8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=Tel_04435 {ECO:0000313|EMBL:ALP52452.1};
OS Candidatus Tenderia electrophaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Candidatus Tenderia.
OX NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP52452.1, ECO:0000313|Proteomes:UP000055136};
RN [1] {ECO:0000313|EMBL:ALP52452.1, ECO:0000313|Proteomes:UP000055136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRL1 {ECO:0000313|EMBL:ALP52452.1};
RA Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA Strycharz-Glaven S.M.;
RT "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL Submitted (OCT-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}.
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DR EMBL; CP013099; ALP52452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2TBF8; -.
DR STRING; 1748243.Tel_04435; -.
DR KEGG; tee:Tel_04435; -.
DR Proteomes; UP000055136; 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:SF46; 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:ALP52452.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055136}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 584
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 927 AA; 105611 MW; 2A7BC8B1EA102368 CRC64;
MDKKLRSRVK LFGNLLGNIL RAQAGDQVFS AVETLRKGYI NLRKEDNAKK QQQLRLLISR
LDPHTLTQVV RAFSIYFSLV NIAEEAYQHQ YRRRLCRFSD GPAWPGSFNA TLNEFKQQNI
SAEQLQTILN RTAYYPVITA HPTEAKRRMV KEALRRIFLT SEELDDTRLS KQERREIIER
LEGEIQILWK TDEVRVRRPR VEDEIRTGIG YFQDCLFDAV PQTYRNMEKA VAKIYAGSPA
VSVPSFLRFG SWVGGDRDGN PNVTPETTRF ALRLQARSVL LEYLNRIGSL TRVLTLSNSL
CRPAEAFTQA LADYDYLVET AFEGDSERFA NEPYRRMLFL MRYRLERNLV AIKHSLGEHV
HEPTEHAYAD EDELLRDLHL IHNSLLSHGD AKIANGTVKD LIRQIETFGF FLMNLDVRQE
STRHSSTVNE VLAQGFGNYN YADMDEDQRL ATLSELIAAK RRPTLARAQL SDETRETLEV
FDVMAQMRDE ISPRAFGTYV ISMTHAASHV MEVMFLAHLA GLVDCDSEQW RCDIEISPLF
ETIEDLAHIE IVMERLLENS TYRRLLAASG DIQEVMLGYS DSCKDGGILA SGWSLYQAQR
KITAIAAKHG IECRLFHGRG GTIGRGGGPT HEAILSQPAG TVFGQIKFTE QGEVLSSKYS
NHETAVYELT MGSTGLLKAS RCIVQEVPGD HDEYLEIIDQ LVRMGEGAYR DLTDDNPALL
DYFYEATPVN EIGMMNIGSR PSHRKQGDRS KDSVRAIAWV FGWAQARHTL PAWYGIGTAL
AQWADNDEQR IATLRQMNRQ WPFFRALLSN TQMALFKADM RIAQEYAQLC LDSDTSATIY
GHVRDEYRQT VDTVLTVTDS DHLLDESPGL ALSLARRNPY LDPLNNIQIT LLKRYRDERQ
PEQERNIWLD PLLRSINAIA AGMRNTG
//