CAPP_VIBPA
ID CAPP_VIBPA Reviewed; 877 AA.
AC Q87L54;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 95.
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=VP2761;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC61024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; BA000031; BAC61024.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_799140.2; NC_004603.1.
DR RefSeq; WP_005465143.1; NC_004603.1.
DR AlphaFoldDB; Q87L54; -.
DR SMR; Q87L54; -.
DR STRING; 223926.28807771; -.
DR EnsemblBacteria; BAC61024; BAC61024; BAC61024.
DR GeneID; 1190311; -.
DR KEGG; vpa:VP2761; -.
DR PATRIC; fig|223926.6.peg.2657; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000002493; Chromosome 1.
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..877
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166648"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 544
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 877 AA; 99273 MW; 3A61D009D5493105 CRC64;
MNEKYAALKS NVRMLGHLLG NTIRDAHGEE IFEKVETIRK LSKSAQAGNQ ADRESLIEEI
KHLPDEQLTP VTRAFNQFLN LTNIAEQYHT ISRHCEEHIC EPDAINSLFS KLVQNDVSKL
DTAQAVRDLN IELVLTAHPT EITRRTMINK LVKINECLSK LELSDLSSKE RKKTERRLEQ
LIAQSWHSDV IRQQRPTPLD EAKWGFAVVE NSLWEAVPDF LREMNDRLKS YLGEGLPIDA
RPVHFSSWMG GDRDGNPFVT HSVTREVLLL SRWKAADLYL NDINELISEL SMTVSNDQVR
ELAGEDQHEP YRAILKQLRA LLNETKDILD AKIHGQKLAV KAPLQKVEQL WDPLYACYQS
LHECGMGVIA DGSLLDTLRR VKAFGVHLVR LDIRQESTRH ADVLSELTRY LGIGDYEQWS
EQDKIAFLTN ELASKRPLLP RDWEPSEPVK EVLDTCKIIA LQPREAFGAY VISMARTASD
VLAVHLLLQE AGCPYRMDVC PLFETLDDLN NAESVIKQLM SIDLYRGFIQ NHQMVMIGYS
DSAKDAGVMS AGWAQYHAME SLVKVAEDEG VELTLFHGRG GTVGRGGAPA HAALLSQPPK
SLKGGLRVTE QGEMIRFKLG LPDVAVNSFN LYASAILEAN LLPPPEPKQE WRDLMEVLSE
VSCEAYRGVV RGEPDFVPYF RQATPELELG KLPLGSRPAK RNPNGGVESL RAIPWIFSWS
QNRLVLPAWL GAGEAIQYSV DKGHQALLEE MCREWPFFST RLGMLEMVYT KCNMEISRYY
DQRLVEPQLQ PLGDRLREQL QRDIKSVLNV ENNENLMQSD PWGQESIRLR NIYVEPLNML
QAELLYRTRQ TEEASANLEE ALMVTIAGIA AGMRNTG