ID   C7C8D0_METED            Unreviewed;       922 AA.
AC   C7C8D0;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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:CAX24132.1};
GN   ORFNames=METD_I2484 {ECO:0000313|EMBL:CAX24132.1};
OS   Methylorubrum extorquens (strain DSM 6343 / CIP 106787 / DM4)
OS   (Methylobacterium extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=661410 {ECO:0000313|EMBL:CAX24132.1, ECO:0000313|Proteomes:UP000008070};
RN   [1] {ECO:0000313|Proteomes:UP000008070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6343 / CIP 106787 / DM4
RC   {ECO:0000313|Proteomes:UP000008070};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
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}.
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; FP103042; CAX24132.1; -; Genomic_DNA.
DR   RefSeq; WP_015822352.1; NC_012988.1.
DR   AlphaFoldDB; C7C8D0; -.
DR   GeneID; 72989458; -.
DR   KEGG; mdi:METDI2484; -.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   Proteomes; UP000008070; 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; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF32; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        581
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   922 AA;  103064 MW;  CB3EDE9D6C3678EC CRC64;
     MTKTLHARPS AATDTTFAPP VITGTATEDA LEILFHALLD VARRHDPELE DVLHGRADIS
     SFTPEMLARA LQVQGIWFQL VSIAEQNAAM RRRRHVERDQ GREALNGSFA KVLAEASARG
     IGPQQIHALL KDLRIRPTIT AHPTEGKRVT VLEKLRRIYL VLRELELPRW TERERNGLMN
     ELRDQIELIW MTGELHLEKA TVEREVAWGL HFFDETLFEM LPEMLLSLEE SLAQYYPDET
     FEVPPFFQFG SWIGGDRDGN PYVTASVTRE TLQRNALASL RRYRDGITHL GRVLSITERS
     LPVPETFRSE LAHMLAESGE ARAIANRNPG EAYRQFLSCV LRKLEATIAR NKGARSVGPD
     YPSADGLIND LRTLEKGLAD AKCGALATDI VRPVRRMVEI FRFSTVRLDL RENSTRTTKT
     LHALWKLRNG DREPPALDSP AWKDWLLTEL ARPRTPETSF EDFADRLPDD ARETLATFAL
     VGEMRDTLDR EAFGAFILSM TRSTVDVLGA YLLAKEAGIF LDTTGTEICP LPIVPLFETI
     DDLRAAPAIM KELLGIPVVR RSTRWQGGVQ EVMIGYSDSN KDGGFIASNW ELYKAQVRLT
     TLGNHLGVPI AFFHGRGGSV SRGGVPTHRG IAAQPPGSIQ GRFRITEQGE VVSFKYANRG
     TAAYQMELLA ASVFEHALLS EGNGNGSRAE FDDALEALSG ASRAAYVNLL QAQGLVDYFQ
     AASPLDEISL LNIGSRPARR FGAKSLSDLR AIPWVFAWSQ NRHVITGWYG VGSGLKSFID
     VRGEAGEALL RRLFRDCRVF RLVLDEVEKT LLMVDLEIAR DYAGLVEDAS IRARIFGMIE
     AEYALTREMV LRVSGDSELA QRFPQFSERL RGRLPTINQV SREQVELLRR YRSETDEDKR
     EAVKSALLLS INCIAVGFGA TG
//