ID H8L338_FRAAD Unreviewed; 902 AA.
AC H8L338;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 OrderedLocusNames=Fraau_0346 {ECO:0000313|EMBL:AFC84836.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC84836.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) 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; CP003350; AFC84836.1; -; Genomic_DNA.
DR RefSeq; WP_014401842.1; NC_017033.1.
DR AlphaFoldDB; H8L338; -.
DR STRING; 767434.Fraau_0346; -.
DR KEGG; fau:Fraau_0346; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000005234; Chromosome.
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:AFC84836.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005234}.
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 569
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 902 AA; 100598 MW; 13E4619746039E4C CRC64;
MDVNRNPEFL AHDGPLREDV HRLGALVGQV LSEQAGESFY EEVEAIRKAS IDRRKQGRPM
DQLSARLGGW AADDAQALAR AFSMYFQAVN MAEMVHRIRR RRDYQRADER PQPESLLDVF
ARLKQNGVGF EELMGWIEKT RIEPVFTAHP TEAMRRSLLD KQKVIVNALI HGFDAGRTPQ
ERRADRSAML TALSAAWQTA ESAATGPSVQ DEHYHVSYYL SHPLYRVVPS LYAQLAEALE
QVYGQSPELP RLLSFATWVG GDMDGNPNVG AETMEASLSA QRSQVLEAYQ ADLQQLESLL
SQTSDRVAVS PAIEQRLHDY AALLPDVDRR IRPRHRNMPY RCLLTYIDAR IEATRDDGAG
AYAGPEPFCD DLALIEASLR GHRGEHAGAR QVRRLRRRAL AFGFHLARLD VRQDSRVHDD
ALAVLLQRPE WVELPASERA QVLGEYAGGT RALPRDAQDA TVQRMQAVFA QLHAMRARYG
VEAAGLYIIS MARSAADVLA VLALARRGGL VQDDGQVPLD IAPLFEIVED LRAAADTLRA
LLADPVYRGH LQARGNRQWV MLGYSDSGKD SGTLAARWAV QRAQVELLEA AREGGIEIAF
FHGRGGSASR GGGRITQALE SSPRGSVAGM LRVTEQGEVI NRKYGIRALA LRNLEQSLGA
VLSASLRPRQ PDVRAPQWRE QMGALANWSR EHYRELVDHP DFVGYFRTAT PIDVIEQMTL
GSRPSRRRSM RGVQDLRAIP WVFAWTQCRS ILTGWYGLGF ALQKGEQVFG LAALQEMARD
WPFFANMLED IEMVLAKCDL DIAEAFSKLS GELHPVFFGR ISEEFERSRD LILRIKGSDR
LLQAQPRLAV SIGLRNPYVD PISLLQVDLL RRWRGEGSQP GPLLEALLAC VNGVSQGLQN
TG
//