ID A0A268EB07_9BACI Unreviewed; 920 AA.
AC A0A268EB07;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=CHH83_04250 {ECO:0000313|EMBL:PAD70289.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD70289.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD70289.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD70289.1,
RC ECO:0000313|Proteomes:UP000216230};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-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|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:PAD70289.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NPCL01000011; PAD70289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268EB07; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000216230; 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; 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.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyruvate {ECO:0000313|EMBL:PAD70289.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216230}.
FT ACT_SITE 150
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT ACT_SITE 578
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 920 AA; 105902 MW; 5ED78A8C75BE3998 CRC64;
MTTRYETNDS SLPLRRDVKS LGHILGEILV HHGGTELLDK VEKLRVMAKT LRNNFDQEIY
NELKEEIVNL DPPMRKQVIR AFSIYFHLIN AAESNHRIRR RREYQLQDNN IVQPASIESA
ILSLKDNEIG VETIQKVLNT LSLELVITAH PTEATKRSVI EIQKRIGNVL KNLDNNMLTK
RERKKLEDSL LNEVTILWQT DELRHRKPTV MDEVRNGLYY FDQTFFEVLP DIHQDLEEGL
TEQFPGHKWE VPNFLRFGSW IGGDRDGNPN VTPEVTWETL EKQRELALKK YREALILAMK
RFSQSTTRVE ISTELIENVE KDEQIYLTED KKWHVENEIY RRKIAVILTR LKEVGKSDIG
YRSAEELLED LYIIQRSVAL HQPANQDLNM LKKLIRQVQL FGFHLATLDI RNHSGEHEAA
ITEILRKVKV AENYSELSEE EKLKTLESVL KDPRPLLLLN EDYTKETQQM IKVFTTIKKA
HDTFGKKSIL VYLVSMTQSA SDLLEVLVLA KEAGIYRLHA DGSVESHLNV APLLETIDDL
VAGPAIMETL FNMDVYRNHL KIHGDSQEIM LGYSDGSKDG GTLTANWKLY KAQLEIHHMA
KRYNIGLKFF HGRGGSLGRG GGPLNRSILS QPAETLGDGV KITEQGEVLS ARYLYEDIAY
RSLEQATSTL LVASVNLSED SEQQHLREKV WEEAMEEISA VSLKKYQSLV FEDPDFLTYF
TEATPLNEVG ELNIGSRPMK RKDRNRFEDL RAIPWVFAWT QSRQLIPAWY AAGTGLEEFA
SKSEENLKLL QRMYLEWPFF RSTIDNLQMA LMKADITTAK EYTSLVKDKT IAERIFGNIV
EEYEKTKEIL LKISGDEELL DHTPNIKESV YRRNPYVDPL NFLQVELIKE LRAQEEPNEE
LLTEVLLTIS GIAAGLRNTG
//