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Database: UniProt/TrEMBL
Entry: A0A0S2TBF8_9GAMM
LinkDB: A0A0S2TBF8_9GAMM
Original site: A0A0S2TBF8_9GAMM 
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
//
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