ID A0A259KDU4_9GAMM Unreviewed; 929 AA.
AC A0A259KDU4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 03-MAY-2023, entry version 18.
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=B7X52_01605 {ECO:0000313|EMBL:OZA97945.1};
OS Thiotrichales bacterium 34-46-19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX NCBI_TaxID=1970605 {ECO:0000313|EMBL:OZA97945.1, ECO:0000313|Proteomes:UP000216156};
RN [1] {ECO:0000313|EMBL:OZA97945.1, ECO:0000313|Proteomes:UP000216156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34-46-19 {ECO:0000313|EMBL:OZA97945.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OZA97945.1}.
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DR EMBL; NCJU01000015; OZA97945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259KDU4; -.
DR Proteomes; UP000216156; 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 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:OZA97945.1}.
FT ACT_SITE 144
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 586
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 929 AA; 106513 MW; 3CBF8E4729C2E42F CRC64;
MKEIQDKQLR ARVKLLGTLL GNVVRQQAGE AVYEAVERLR QGYISLRKQD DPALRQSLND
FIAELDADTM THVIRAFNIY FGLANLAEEE GAFHRRQHQM REEGPLWLGS FMTSIGELKA
EGISAEQMNE LVQGLMYRPV FTAHPTESKR RAVMENLREV FVTLEDLVFD ERRNDWNDPE
IINRLQTQIQ VLWNTDEVRS TKPEVDDEIR HGIFYFRQSL FEAVPKVYRF MDRALAHHYP
EAKLSASPFL SFGSWIGGDR DGNPFVTHQK TEMAVLLHAR TILYYYRDTV FKLSRHLTHS
RHLCNISQEV INRATIVDSD LLHEIFHNRP NRFSDEPYRR FLYIIEGRIQ ATLSWIESRI
NKEPAPRSRF AYDNEYQFLE DLQLIHDSLC GHGDKTIADS DLLDLIRVVK TFGFYLMRLD
IRQESTVHSE SVAELLMHLG IDYNALTEEA RIRLLAEHIA SPVIIDRKHL VLSEKTKEVL
AVFDVIRQMR EEISPKAFGQ YVISMTHHAS HVMEVMFLAH QTGLAGASNG ETYCHIQVSP
LFETIEDLQH IVPVMTDLME NETYRALVNS AGKLQEIMLG YSDSCKDGGI VASAWNLYRA
QKEIMAVFDQ YDIECRLFHG RGGTVGRGGG PTHIAIQSQP YGTVHGQIKF TEQGEVLSYK
YSNSETAAYE LTLGVTGLMK ASTHLVQSVR VEDEQDMAIM AELAQYGEAS YRQLTDNTPG
FLDYFYEITP VTEIGLLNMG SRPSHRKTGN RSKASIRAIP WVFGWAQARL TLPAWYGLGS
ALDQWQKEHP EQPTALRDMY ERWPFFRSMV SNIQMSLFKT ELTTGKEYSM LAQDREQALS
IYDTIAGEYH CTSKQVLSIS GNETLMADTP EIALSLHRRN PYLDPLNHVQ IVLLKRYRNP
EATEAERDMW LRPLLRSINA IAAGMRNTG
//
