ID   CAPP_MYCUA              Reviewed;         935 AA.
AC   A0PPN8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=MUL_1836;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CP000325; ABL04307.1; -; Genomic_DNA.
DR   RefSeq; WP_011739927.1; NC_008611.1.
DR   AlphaFoldDB; A0PPN8; -.
DR   SMR; A0PPN8; -.
DR   STRING; 362242.MUL_1836; -.
DR   EnsemblBacteria; ABL04307; ABL04307; MUL_1836.
DR   KEGG; mul:MUL_1836; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000000765; 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   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; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..935
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025567"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   935 AA;  102784 MW;  4A790C15C4CFB92D CRC64;
     MVEVSDTALE PIGDVHRTRI GREATEPMRA DIRLLGAILG DTVREQNGDE VFELVERARV
     EAFRVRHSEI DRAEMARMFE GIDIHHAIPI IRAFSHFALL ANVAEDIHRE RRRSIHVAAG
     EPPRDSSLTA TYMKLYAAQL DSATIAEALK GALVSPVITA HPTETRRRTI FETQHRITQL
     MRLHAEGHTE TDDGRGIEVE LRRQVLRLWQ TALIRLFRLQ ISDEIEVGLR YYPAALFEVI
     SQVNAEVRDA LRARWPDADL LSEPILRPGS WIGGDRDGNP NVTAEVVRLA TGSAAFTALA
     HYLAELTALA QELSMSARLI TVTPELATLA DACPAGARPD EPYRRALQVV RGRLSATAAE
     ILDQQPQHTL ELGLPPYATA AELRADLDTI DASLHNHGAG LLADDRLARL REAVRVFGFH
     LSGLDMRQNS DVHEQVVGEL LAWAGVHPDY TSLAEAERVE LLAAELSTRR PLIRDGAQLS
     DLARSELGVL AAAAHAVWTF GPAAVPNYII SMCWSVSDML EAAVLLKEVG LLDASESEPY
     CPVGISPLFE TIEDLHNGAA ILQAMLDLPL YRALVTARGG CQEVMLGYSD SNKDGGYLAA
     NWAVYRAELA LVETARKTGI RLRLFHGRGG TVGRGGGPSY QAILAQPPGA VSGSLRLTEQ
     GEVIAAKYAE PQMARRNLES LLAATLESTL LAVEGLGDTA APAYAVLDEV AALAQRAYAE
     LVHETPGFVE YFKASTPVSE FGALNIGSRP TSRKPTASIA DLRAIPWVLA WSQSRVMLPG
     WYGTGSAFEQ WLAAGPESEA DRLQVLHDLY QRWPFFRSVL SNMAQVMAKS DLELAARYSE
     LVADETLRRR VFDKIADEHH RTIAMYKRIT GQDDLLADNP ALARSVFNRF PYLEPLNHLQ
     VELLRRYRSG EDDESVQRGI LLTMNGLASA LRNSG