ID   CAPP_MYCPA              Reviewed;         935 AA.
AC   P61449;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=MAP_1169;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03486.1; -; Genomic_DNA.
DR   RefSeq; WP_003877648.1; NZ_CP106873.1.
DR   AlphaFoldDB; P61449; -.
DR   SMR; P61449; -.
DR   STRING; 262316.MAP_1169; -.
DR   KEGG; mpa:MAP_1169; -.
DR   PATRIC; fig|262316.17.peg.1230; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000000580; 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; IPR033129; PEPCASE_His_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; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..935
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166601"
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;  102599 MW;  E9EF1E7F12D5BF0C CRC64;
     MVEASEGTLE PIGAVQRTLV GREATEPMRA DIRLLGAILG DTVREQNGQQ VFELVERARV
     ESFRVRRSEI DRAELARMFA GIDIHQAIPV IRAFSHFALL ANVAEDIHRE RRRAIHVAAG
     EPPQDSSLAA TYAKLDRAQL DSAMVAEALR GAVVSPVITA HPTETRRRTV FVTQHRITEL
     MRLHAEGHTE TDDGRNIELE LRRQVLTLWQ TALIRLSRLQ ITDEIEVGLR YYAAAFFKVI
     PQVNAEVRNA LRARWPGADL LDEPIVAPGS WIGGDRDGNP NVTADVVRRA TGDAAYTALA
     HYLAELTACE QELSMSARLV AVTPELAALA EDCAEKARAD EPYRRALRVI RGRLTATAAE
     ILDRRPQHEL DLGLPPYATP AELRADLDTV DASLRAHGSA LLADDRLALL REGVRVFGFH
     LCGLDMRQNS DVHEEVVAEL LAWAGVHPDY RSLPEDERVE LLAAELGTRR PLVGDRAELS
     ELADKELGVV RAAAHAIRRY GPAAVPNYVI SMCRSVSDVL EAAILLKEAG LIDASGPEPY
     CPVGISPLLE TIEDLHNGAA ILHAMLELPL YRALVAARGQ SQEVMLGYSD SNKDGGYLAS
     SWAVYRAELA LVEVARKIGI RLRLFHGRGG TVGRGGGPSY EAILAQPPGA VNGSLRLTEQ
     GEVIAAKYAE PQVAQRNLES LVAATLESTL LDVEGLGDTA EPAYAVLDEV AVLAQRAYAE
     LVHETPGFVD YFMASTPVSE IGSLNIGSRP TSRKPTESIA DLRAIPWVLA WSQSRVMLPG
     WYGTGSAFEQ WIAAGPQSRA ERVDILHDLY RRWPFFRSVL SNLAQVLAKS DLGLAAQYAE
     LVDDAALRRR VFGKIADEHR RTIAMHKLIT GQDNLLADNP ALARSVFNRF PYLEPLNHLQ
     VELLRRYRSG DDDELVQRGI LLTMNGLASA LRNSG
//