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Database: UniProt/TrEMBL
Entry: U4KHH5_9VIBR
LinkDB: U4KHH5_9VIBR
Original site: U4KHH5_9VIBR 
ID   U4KHH5_9VIBR            Unreviewed;       877 AA.
AC   U4KHH5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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:CCO59569.1};
GN   ORFNames=VIBNI_A3596 {ECO:0000313|EMBL:CCO59569.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO59569.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO59569.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA   Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT   identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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,
CC         ECO:0000256|HAMAP-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}.
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DR   EMBL; FO203526; CCO59569.1; -; Genomic_DNA.
DR   RefSeq; WP_022551978.1; NC_022528.1.
DR   AlphaFoldDB; U4KHH5; -.
DR   STRING; 28173.VIBNI_A3596; -.
DR   KEGG; vni:VIBNI_A3596; -.
DR   PATRIC; fig|1260221.3.peg.3415; -.
DR   eggNOG; COG2352; Bacteria.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000016895; 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   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; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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};
KW   Pyruvate {ECO:0000313|EMBL:CCO59569.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016895}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   877 AA;  98706 MW;  6EA8DA3E93C20D9E CRC64;
     MNEKYAALKS NVSMLGRLLG NTIQDAHGEA ILEKVETIRK LSKSAMAGGQ EDRENLIKEI
     ESLPDEQLTP VARAFNQFLN LTNMAEQYHT ISRHCEEHVC EPDALNSLFS KLSQNSISKL
     DTAQAVRDLN IELVLTAHPT EITRRTMINK LVKINECLSK LELSDLSYKE RQKTERRLEQ
     LIAQAWHSDV IRQQRPTPLD EAKWGFAVVE NSLWQGVPDF LRELDEKLEG YLDEGLPIDA
     RPVHFSSWMG GDRDGNPFVT HTITREVMLL SRWKAADLYL NDINELVSEL SMTKCSDVLR
     ELAGEGQHEP YRAILKRIRD VLTETRDILE AKINGEQLAV KAPLKSVDQL WEPLHACYQS
     LHECGMGVIA DGSLLDTLRR IKAFGIHLVR LDIRQESTRH SDVLSELTRY LGIGDYDQWS
     EQDKVAFLTA ELSSKRPLLP RDWEPSEPVK EVLDTCRIVA SQPREAFGAY VISMARTASD
     VLAVHLLLQE SGCPYRMDVC PLFETLDDLN NAEAVITQLM GIDLYRGFIQ NHQMVMIGYS
     DSAKDAGVMA AGWAQYRAME ALVKVSEEAG IELTLFHGRG GTVGRGGAPA HAALLSQPPK
     SLKGGLRVTE QGEMIRFKLG LPEVAVNSFN MYASAILEAN LLPPPEPKQE WRDLMDVLSE
     VSCEAYRGVV RGEPDFVPYF RAATPELELG MLPLGSRPSK RNPKGGVESL RAIPWIFSWS
     QNRLVLPAWL GAGEAIQYSV DKGHQSLLEA MCREWPFFST RLGMLEMVYS KCNIEISRLY
     DQKLTDESLW PLGDKLRAQL QKDIKAVLNV ENNENLMQSD PWGLESIRLR NIYVEPLNML
     QAELLYRTRQ TETPSSELEE ALMVTIAGIA AGMRNTG
//
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