CAPP_PROMH
ID CAPP_PROMH Reviewed; 878 AA.
AC B4F183;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=PMI3227;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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}.
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; AM942759; CAR46321.1; -; Genomic_DNA.
DR RefSeq; WP_004246402.1; NC_010554.1.
DR AlphaFoldDB; B4F183; -.
DR SMR; B4F183; -.
DR STRING; 529507.PMI3227; -.
DR PRIDE; B4F183; -.
DR EnsemblBacteria; CAR46321; CAR46321; PMI3227.
DR GeneID; 6801836; -.
DR KEGG; pmr:PMI3227; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000008319; 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; Reference proteome.
FT CHAIN 1..878
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000129836"
FT ACT_SITE 137
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 545
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 878 AA; 98678 MW; 208C42D3EA1C9AA3 CRC64;
MNQQYSAMRS NVSMLGKLLG DTIKEALGEE ILDKVESIRK LSKSSRAGNE VQRQKLLLTL
QNLSNDELLP VARAFNQFLN LTNVAEQYHS ISPHGEAASN PVALAKLIER LKDKNFTNQQ
LKQAVEQISI ELVLTAHPTE IARRTLIHKL VEVNTCLSQL DHDDLADYER TNIMRRLRQL
VAQSWHTDEI RKIRPTPIDE AKWGFAVVEN SLWEGVPAFL REFNEQLEES IDYNLPVEAS
PIRFTSWMGG DRDGNPNVTA EITRHALLLS RWKAADLFLN DIQVLVSELS MTESTPELRE
LAGGADVAEP YREIAKQLRT RLQVTRDYLE QRIKGQQSLP PEGLLIDNSA LWEPLYACYQ
SLHQCGMRII ANGQLLDTLR RIRCFGLQLV RLDIRQESTN HTEALSELTQ YLELGDYASW
SEEQKQTFLL TELNSKRPLI PTHWQPSEAT KEVFETCRVI AESPKDSIAS YVISMAKVPS
DVLAVKLLLK EAGADIRLPV APLFETLEDL NNAESVMTRL FDIPWYRDLI DNKQMVMIGY
SDSAKDAGVM AASWAQYRAQ DALIKLCEKS GVTLTLFHGR GGTIGRGGAP AHAALLSQPP
GSLKGGLRVT EQGEMIRFKF GLPQVTISSL AHYAGAILEA NLLPPPEPKT AWIEVMDALS
DVSCEMYRGY VRGEKDFVPY FRAATPEGEL GKLPLGSRPA KRRPTGGVET LRAIPWIFAW
TQNRLMLPAW LGAGAALQHE IDNGKQAVLD DMCENWPFFN TRIAMLEMVY AKADLWLAEY
YDQRLVEENL WPLGAKLRQQ LSDDIKSVLA ISKDEHLMAD LPWVAESIAL RNVYTDPLNV
LQAELLQRSR THSESDPRIE QALMVTIAGI AAGMRNTG