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
//