ID   I0JJ14_HALH3            Unreviewed;       919 AA.
AC   I0JJ14;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   OrderedLocusNames=HBHAL_1767 {ECO:0000313|EMBL:CCG44132.1};
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 /
OS   KCTC 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44132.1, ECO:0000313|Proteomes:UP000007397};
RN   [1] {ECO:0000313|EMBL:CCG44132.1, ECO:0000313|Proteomes:UP000007397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC   NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT   salinities by the moderately halophilic, chloride-dependent bacterium
RT   Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
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; HE717023; CCG44132.1; -; Genomic_DNA.
DR   RefSeq; WP_014642036.1; NC_017668.1.
DR   AlphaFoldDB; I0JJ14; -.
DR   STRING; 866895.HBHAL_1767; -.
DR   KEGG; hhd:HBHAL_1767; -.
DR   PATRIC; fig|866895.3.peg.764; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000007397; 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:UP000007397}.
FT   ACT_SITE        150
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        577
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   919 AA;  106039 MW;  00216DEAAA6B1FAC CRC64;
     MTNQPKTNDH TTPLRRDINE LGKMLGNLLV HHGGEELLNK VETIRQLTKD LRNNHSTSTY
     NQLKEEIQNL KPPMRSQVIR AFSIYFHLVN IAEQNHRIRR RREYQLREDH GAQPFSLESA
     VLNLKNNNFS KDVIQNVLDH LSLELIITAH PTEATKRTVL EIQKRIATIL QKLDNPQLTK
     NERDSLKDSL QNEVSVLWQT DELRDRKPTV MDEVRNGLYY FDETLFDVLP EIHQELEYCL
     EENYPEEDWD VPNFLRFGSW IGGDRDGNPN VTPDITWQTL QKQRNLVLNK YEEVLVELMK
     RFSHSSAQVT VTDELMASIE KEEPQLPKGK KWRVEKEIYR RKFAIVLERL RQVGQSDLGY
     DYADELLEDL YQIQKSAKTH QPARRELKKL RKLIRQVELF GFHLATLDIR NHSGEHESAV
     DELLRKVSIE DNYSELAEDK KIEVLQNVLK DPRPISLLNE DYSDSTQEML TVFQMIRNAH
     IEFGKRSIEV YLISMTESAS DLLEVLVLAK EAGIYRLHAD GTVESNINVA PLLETVDDLV
     AGPEILKTLF EMDVYAKHLK HRNNHQEIML GYSDGSKDGG TLTANWRLYK AQQEIHTMAR
     EYNVGLKFFH GRGGSLGRGG GPLNRSLLSQ PEETLGDGVK ITEQGEVLSS RYLIKDIAYR
     SLEQGASTLL EGAANVSQES EQAHNREDAW EQAMEEIAEI SLKKYQSLVF GDKDFLTYFN
     EATPLKEISE LNIGSRPMKR KDSSKFENLR AIPWVFAWSQ NRQLIPAWYA AGSGLASYVE
     NDNDRLEQLK QMYINWPFFR STINNLQMAL TKADIQTAQE YTQLVNDQEL GERIFNNIVD
     EYERTKEILL KISGDEELLT HQPTIKESVR LRNPYVDPLN FLQVELIKEL RASEDQDDEL
     LTEVLLTISG IAAGLRNTG
//