CAPP_ALIFM
ID CAPP_ALIFM Reviewed; 876 AA.
AC B5FBP8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=VFMJ11_2420;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001139; ACH67224.1; -; Genomic_DNA.
DR RefSeq; WP_005421129.1; NC_011184.1.
DR AlphaFoldDB; B5FBP8; -.
DR SMR; B5FBP8; -.
DR EnsemblBacteria; ACH67224; ACH67224; VFMJ11_2420.
DR GeneID; 64243728; -.
DR KEGG; vfm:VFMJ11_2420; -.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000001857; Chromosome I.
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.
FT CHAIN 1..876
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000129846"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 543
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 876 AA; 99011 MW; E7C7671A941C8AC1 CRC64;
MNEKYAALKS NVSMLGHLLG NTIRDAHGEE LLAKVETIRK LSKTARAGSD EDRNALIEEI
KSLPDDQLTP VARAFSQFLN LTNMAEQYHT ISRHCEAHVC EPDAISTLFS KLSQSNVSKL
DTAQAVRELN IELVLTAHPT EIARRTMINK LVKINECLSK LELGDISFSE RDKTERRLEQ
LIAQAWHSDV IRQERPTPLD EAKWGFAVVE NSLWQGIPEF LREFDQRLEG HLGEGLPIDA
RPVHMSSWMG GDRDGNPFVT HKITREVMLL SRWKAADLYL KDINELISEL SMVKCTDEVR
ELAGDQHEPY RAILKQLRTL LGDTLESLDA QMKGELVPNK AILTDADQLW NPLYACYQSL
HACGMGIIAD GSLLDTLRRV KAFGAHLVRL DIRQESTRHS DVLSELTRYL GIGDYDQWSE
QDKISFLVNE LSSKRPLLPR KWEPSPEVQE VIDTCRVVAE QSKEALGSYV ISMARTASDV
LAVHLLLQEA GCPFRMDVCP LFETLDDLNR SKEVMEQLFS IDWYRGFIQN HQMVMIGYSD
SAKDAGVMSA GWAQYSAMEA LVEVCEKESI ELTLFHGRGG TIGRGGAPAH AALLSQPPKS
LKGGLRVTEQ GEMIRFKLGL PEVAVNSFNL YASAILEANL LPPPEPKQEW RDLMEVLSEV
SCEAYRNVVR GEKDFVPYFR AATPELELGK LPLGSRPAKR NPNGGVESLR AIPWIFSWSQ
NRLVLPAWLG AGEAIQYSID KGHQELLEEM CREWPFFSTR LGMLEMVYTK CNPQMSEYYD
QRLTDKSLWP LGERLRNQLQ TDIKAVLNVE NNDHLMERDP WGSESIRLRN IYVDPLNMLQ
AELLFRTRQQ EETSPELEEA LMVTIAGIAA GMRNTG