ID   F8CRX5_MYXFH            Unreviewed;       889 AA.
AC   F8CRX5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=LILAB_30860 {ECO:0000313|EMBL:AEI68053.1};
OS   Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI68053.1, ECO:0000313|Proteomes:UP000000488};
RN   [1] {ECO:0000313|EMBL:AEI68053.1, ECO:0000313|Proteomes:UP000000488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX   PubMed=21868801; DOI=10.1128/JB.05516-11;
RA   Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT   "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT   1.";
RL   J. Bacteriol. 193:5015-5016(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}.
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; CP002830; AEI68053.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8CRX5; -.
DR   STRING; 483219.LILAB_30860; -.
DR   KEGG; mfu:LILAB_30860; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_7; -.
DR   Proteomes; UP000000488; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:AEI68053.1}.
FT   ACT_SITE        150
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        556
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   889 AA;  98303 MW;  4DB86CAFD2C29B52 CRC64;
     MARLRAVDQP LRRDVRLLGR LLGEVLVEQE GQALFDLEEE VRRLAIQRRR GPMAGRRAVA
     AELAEVLQRL PLAQAEPVLR AFSVYFQLVN LAEQHHRIRR ARTHAEAASA RPQRGSLEST
     LLALKAAGVP ARRVREAMKA MRVTLTLTAH PTQAVRRTLL EKLYRMAGLL EQRDRSALTP
     REGALNLALL REEITLLWQT DELRRERPTV GDEVKNVLWY VEEVLADELS LLPELLDWAF
     ERAYGEPLGP VDTPVRIHSW VGGDMDGNPL VTPDVFADTL RAHRARGLRR LLLDLERLGG
     RLSQSERHAK PSEELLASVA RDAEALPEAE RRYGPRTPGE PLRHKLRFME ERLHRALHYV
     TQQRAGARIP MPPGAYRTPE ALLADLDVLG RALEASKGAH AGLRDVRQVR ERVLALGLSL
     AELEVRAPAE DAVSAAGSFN GGPAPTEGGA RLLEVLARLK EAQSESGEPA CRTLILSMAS
     TAEDVLAAFQ CLQHAGLWDE VRGCATVDVV PLFEQLGALD SGPDVLRTLF ADAAYRKHLD
     ARGGQEVMVG YSDSGKEVGL LAASAALYRA QVALTEVSRE AGVPLRLFHG RGESVARGGG
     PAQEAILALP PGAVAGGYKA TEQGEALDHK YARPELARRT LELILGGVLL HTLDAQPRPA
     PEAERTFRTA FDTLAETGRK AYRALVWEDP RFLEFFTAAT PVEEIASLPI GSRPSKRKAG
     GLETLRAIPW VFAWTQNRAI LPGWYGVGSA LEAFSKEEGG AALLKRMYRE WPFFRAVIDN
     VTMVLAKSDM AIAGRYATLA PAATRSLWRR IQQEHRRTRK QVKRLTGESK LLDNNPQLQR
     SISLRNPYVD PMSFLQVELL KRKREGQAEV DRPLLLTLNG IAAGMRNTG
//