ID   D3FXB2_ALKPO            Unreviewed;       918 AA.
AC   D3FXB2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
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   Synonyms=pepC {ECO:0000313|EMBL:ADC50623.1};
GN   OrderedLocusNames=BpOF4_12860 {ECO:0000313|EMBL:ADC50623.1};
OS   Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS   (Bacillus pseudofirmus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX   NCBI_TaxID=398511 {ECO:0000313|EMBL:ADC50623.1, ECO:0000313|Proteomes:UP000001544};
RN   [1] {ECO:0000313|EMBL:ADC50623.1, ECO:0000313|Proteomes:UP000001544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2126 / JCM 17055 / OF4
RC   {ECO:0000313|Proteomes:UP000001544};
RX   PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA   Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA   Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA   Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA   Hu F.Z., Krulwich T.A.;
RT   "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT   support the ability to grow in an external pH range from 7.5 to 11.4.";
RL   Environ. Microbiol. 13:3289-3309(2011).
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; Evidence={ECO:0000256|HAMAP-
CC         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; CP001878; ADC50623.1; -; Genomic_DNA.
DR   RefSeq; WP_012957987.1; NC_013791.2.
DR   AlphaFoldDB; D3FXB2; -.
DR   STRING; 398511.BpOF4_12860; -.
DR   KEGG; bpf:BpOF4_12860; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000001544; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000001544}.
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        576
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   918 AA;  105235 MW;  AE8C5687D132636E CRC64;
     MIEVNDANTL LRNDVKKLGN ILGEILVHHG GVDLLNKVES IREKTKSLRQ HHDQETYNAL
     KEEIATLEPP TRQQVIRAFS IYFHLVNIAE QNHRIRRQRQ YQLNEEGVSQ PFSLERAVSA
     VKELQPEDAV MQKVLNDLSI ELIITAHPTE ATKRTVLETQ KRISTILQEF DNQQLTKKER
     RRLEDSLFNE VTALWQTDEL RHRKPTVLDE VKNGLHYFNQ TLFEVIPEVH QELEVQLDEQ
     FPNHKWSVPN FLHFGSWIGG DRDGNPNVTP EVTWETLKLQ RRLVLKKYKE SLVDLMKRFS
     QTTTRVQISD ELLQSVEADE ANYLEDGEEW PIETELYRRK FQVILKRIRA VGKEDKAAYQ
     NAEELLADLN LIKESAEQHQ PANRTLKTLR KLIRQVQLFG FHLATLDIRN HSGEHEAAIT
     EILRAVQITD DYASLTEEEK LTILQDVLRD PRPLLLLKED YSKETQEVIK VFDMIKQAHR
     EFGSRSIEVY LVSMTQSSSD LLEVLLLAKE AGIYRLHADG TVDSGLHVAP LLETVDDLVA
     GPRIMKTLFE MDVYRNHLSE RGNHQEIMLG YSDGSKDGGT LTANWKLFKA QQEIHDMAKD
     YQVRLKFFHG RGGSLGRGGG PLNRSILSQP AETLGDGVKI TEQGEVLSSR YLLEDIAYRN
     LEQAASALLE ASASSQIQTK KGHSRKEAWE EAMEEASKHS LKKYQSLVFG DQDFLTYFKQ
     ATPLNELGAL NIGSRPMSRK GSQRFEDLRA IPWVFAWTQS RQMIPAWYAA GTGLSAFANE
     SEENLALLRE MYNNWPFFHS TINNLQMALM KADLKTAKEY MNLVEDQEIA DRIFGDISEE
     YIRTKEILLK ISESEELLDH SPNIQESVHR RNPYVDPLNF LQVDLISKMR AEENPSDELM
     TEVLLTISGV AAGLVNTG
//