ID   B2HP92_MYCMM            Unreviewed;       935 AA.
AC   B2HP92;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
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:ACC40696.1};
GN   OrderedLocusNames=MMAR_2247 {ECO:0000313|EMBL:ACC40696.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40696.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC40696.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, 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; CP000854; ACC40696.1; -; Genomic_DNA.
DR   RefSeq; WP_012394005.1; NC_010612.1.
DR   AlphaFoldDB; B2HP92; -.
DR   STRING; 216594.MMAR_2247; -.
DR   KEGG; mmi:MMAR_2247; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001190; 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 {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:ACC40696.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   935 AA;  102668 MW;  A25AC95BF2D2A2C7 CRC64;
     MVEVSDTALE PIGDVHRTRI GREATEPMRA DIRLLGAILG DTVREQNGDE VFELVERARV
     EAFRVRHSEI DRAEMARMFE GIDIHHAIPI IRAFSHFALL ANVAEDIHRE RRRSIHVAAG
     EPPQDSSLAA TYMKLDAAQL DSATIAEALK GALVSPVITA HPTETRRRTI FETQHRITQL
     MRLHAEGHTE TDDGRGIEVE LRRQVLRLWQ TALIRLFRLQ ISDEIEVGLR YYPAALFEVI
     PQVNAEVRDA 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 SMCRSVSDML EAAVLLKEVG LLDASESEPY
     CPVGISPLFE TIEDLHNGAA ILQAMLDLPL YRALVTARGG CQEVMLGYSD SNKDGGYLAA
     NWAVYRAELA LVETARKTGI RLRLFHGRGG TVGRGGGPSY QAILAQPPGA VSGSLRLTEQ
     GEVIAAKYAE PQMARRNLES LLAATLESTL LDVEGLGDTA APAYAVLDEV AALAQRAYAE
     LVHETPGFVE YFKASTPVSE IGALNIGSRP TSRKPTASIA DLRAIPWVLA WSQSRVMLPG
     WYGTGSAFEQ WLAAGPESEA DRLQVLHDLY QRWPFFRSVL SNMAQVMAKS DLELAARYSE
     LVADETLRRR VFDKIADEHH RTIAMYKRIT GQDDLLADNP ALARSVFNRF PYLEPLNHLQ
     VELLRRYRSG EDDESVQRGI LLTMNGLASA LRNSG
//