CAPP_METEA
ID CAPP_METEA Reviewed; 922 AA.
AC Q49136; C5B112; P71502;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=ppc; Synonyms=ppcA; OrderedLocusNames=MexAM1_META1p1732;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9168622; DOI=10.1099/00221287-143-5-1729;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Molecular and mutational analysis of a DNA region separating two
RT methylotrophy gene clusters in Methylobacterium extorquens AM1.";
RL Microbiology 143:1729-1736(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=7961516; DOI=10.1128/jb.176.23.7398-7404.1994;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Genetics of the serine cycle in Methylobacterium extorquens AM1:
RT identification, sequence, and mutation of three new genes involved in C1
RT assimilation, orf4, mtkA, and mtkB.";
RL J. Bacteriol. 176:7398-7404(1994).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; U72662; AAB58883.2; -; Genomic_DNA.
DR EMBL; CP001510; ACS39576.1; -; Genomic_DNA.
DR EMBL; L33465; AAA62656.1; -; Genomic_DNA.
DR PIR; D55230; D55230.
DR RefSeq; WP_003597630.1; NC_012808.1.
DR AlphaFoldDB; Q49136; -.
DR SMR; Q49136; -.
DR STRING; 272630.MexAM1_META1p1732; -.
DR EnsemblBacteria; ACS39576; ACS39576; MexAM1_META1p1732.
DR KEGG; mea:Mex_1p1732; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_5; -.
DR OMA; GPTHRFI; -.
DR OrthoDB; 398146at2; -.
DR BioCyc; MetaCyc:MON-3824; -.
DR Proteomes; UP000009081; 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 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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium.
FT CHAIN 1..922
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166599"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10112"
FT ACT_SITE 581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10112"
FT CONFLICT 28
FT /note="E -> A (in Ref. 3; AAA62656)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="D -> E (in Ref. 1; AAB58883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 103021 MW; 11B90AD09BB5683E 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 LAHMLAESGD 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 QAEGLVDYFQ
AASPLDEISL LNIGSRPARR FGAKSLSDLR AIPWVFAWSQ NRHVITGWYG VGSGLKSFID
VRGEAGEALL RRLFRDCRVF RLVLDEVEKT LLMVDLEIAR DYAGLVEDAG IRARIFGMIE
AEYALTREMV LRVSGDSELA QRFPQFSERL RGRLPTINQV SREQVELLRR YRSETDEDKR
EAVKSALLLS INCIAVGFGA TG
