ID   Q1D3N4_MYXXD            Unreviewed;       889 AA.
AC   Q1D3N4;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 126.
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   ECO:0000313|EMBL:ABF88461.1};
GN   OrderedLocusNames=MXAN_4571 {ECO:0000313|EMBL:ABF88461.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF88461.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF88461.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF88461.1; -; Genomic_DNA.
DR   RefSeq; WP_011554566.1; NC_008095.1.
DR   AlphaFoldDB; Q1D3N4; -.
DR   STRING; 246197.MXAN_4571; -.
DR   EnsemblBacteria; ABF88461; ABF88461; MXAN_4571.
DR   GeneID; 41361872; -.
DR   KEGG; mxa:MXAN_4571; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_7; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002402; 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   Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT   REGION          303..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  98823 MW;  CAB65D7A7B5E3110 CRC64;
     MARLRAVDQP LRRDVRLLGR LLGEVLVEQE GQALFDLEEE VRRLAIQRRR GPVAGRRAVA
     AELAEVLQRL PLERAEPVLR AFSVYFQLVN LAEQHHRIRR ARTHAEVASA KPQRGSLEAT
     LQVLKEAGIP AERVREAMRT MRVTLTLTAH PTQAVRRTLL EKLYRMAGLL EERDRCELTP
     RESSVNLALL REEITLLWQT DELRRERPTV GDEVKNVLWY VEEVLADELS LLPELLDWAF
     ERAYGEPLGP VDTPVRIHSW VGGDMDGNPL VTPDVFADTL RAHRARGLRR LLLDLERLGG
     RLSQSARHAK PSEELLSSVA KDAEELPDTE RRYGPRTPGE PLRHKLRFME ERLHRALHYV
     TQQRAGTSVP MPQGAYRTPE ALLADLDVLG RALEASKGTH AGLRDVRQVR ERVLALGLSL
     AELEVRAPAE DAVSAAGSFN GGPAPTEGGA RLLEVLARLK EAQSESGESA CRTLILSMAS
     TAEDVLAAFR CLKHAGLWDE KRGCATANVV PLFEQLGALD SGPDVLRTLF ADAEYRKHLD
     VRGGQEVMVG YSDSGKEVGL LAASAALYRA QVALTEVSRE AGVPLRLFHG RGESVARGGG
     PAQEAILALP PGAVAGGYKA TEQGEALDHK YARPELARRT VELILGGVLL HTLDAQPRPE
     PEAERTFRTV FDTLAETGRK AYRALVWEDP RFLEFFTAAT PVEEIASLPI GSRPSKRRAG
     GLDTLRAIPW VFAWTQNRAI LPGWYGVGSA LEAFSKEEGG AAQLKRMYQE WPFFRAVIDN
     VTMVLAKSDM AIAGRYASLA PPATRSLWRR IQQEHRRTRR QVKRLTGESK LLDNNPQLQR
     SISLRNPYVD PMSFLQVELL KRKREGQAEV DRPLLLTLNG IAAGMRNTG
//