ID A0A1Y6HK95_9XANT Unreviewed; 904 AA.
AC A0A1Y6HK95;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=PD5205_00943 {ECO:0000313|EMBL:SMR02262.1};
OS Xanthomonas fragariae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=48664 {ECO:0000313|EMBL:SMR02262.1, ECO:0000313|Proteomes:UP000195953};
RN [1] {ECO:0000313|EMBL:SMR02262.1, ECO:0000313|Proteomes:UP000195953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD5205 {ECO:0000313|EMBL:SMR02262.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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; LT853885; SMR02262.1; -; Genomic_DNA.
DR RefSeq; WP_002811904.1; NZ_ORZZ01000182.1.
DR AlphaFoldDB; A0A1Y6HK95; -.
DR STRING; 48664.BER92_04560; -.
DR GeneID; 61895366; -.
DR KEGG; xfr:BER92_04560; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000195953; 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:SMR02262.1}.
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 570
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 904 AA; 99969 MW; D9CECBDAD365BF80 CRC64;
MNEYRSSLVF ATPDLPLRDD VRRLGALVGD LLAEQVSMEF LEEIERVRTT AISRRESDAP
PSTLSAQLSG REPRQAEALV RAFSTYFQVV NIAERVHRIR RRRQYQRSST DTPQPDGLHD
ALRRLMAQGV TLQELSDWLP RIDVEPVFTA HPTEAVRRAL LEKEQLMVAS LVANLDGMRT
PNESATDAAR FRMALTASWQ TADSSPVRPT VEDEREHVGF YLTQVLYRVV PVVYETLEHA
IEETYGSVRA LPRLLRFGTW VGGDMDGNPN VDAATIAGTL DAQRRAVLDR YRKELWQLAS
LLSQSTTLVA VSPALSEQLE RYRTLLPDAA ARSRPRHGDM PYRLLNDLMR ARLQATLDDA
EGAYGAPSQL EHDLQLILDS LQANKGLHAG WFAVRRLLWR VRTFGFHLAR LDVRQESSVH
ACAVADALGQ ADWNAQDAKQ RAALLGPYAS GEQALPRVQD EGNARLDAVF AALADARTCH
GADALGSYII SMAHNRADVL TVLALARRGG LVDDAGAVPL DIVPLFETVA DLRGGTGTVQ
DLLADPVYRQ HLAARGDTQM VMLGYSDSGK DGGIAASRWG LQRAQVELLE AAAELGVRLT
FFHGRGGSIA RGGGKTSRAL DAAPRGSVDG RLRVTEQGEV IHRKYGIRAL ALRSLEQMTG
AVLLSSLRPR APEPREDRWR PVMDLVAERS TVAYRAFVGA PDFMQYFRLA TPIDVIERMT
LGSRPSRRLG QDAALSNLRA IPWVFAWSQA RAVIPGWYGV GSGLQAAVDA GHEDSLREMA
RDWPFFRTFL DDVAMVLSKG DLTIAELFSR LSGDLHTRFF PGIRDELALT KGWVKALTGQ
QSLLQHDPRL ALSIRLRNPY IDPISVLQVD LLQRWRATDG EDEELLRALV ACVNGVSQGV
QNTG
//
