CAPP_PARXL
ID CAPP_PARXL Reviewed; 994 AA.
AC Q143B6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Bxeno_A1035;
GN ORFNames=Bxe_A3412;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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}.
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DR EMBL; CP000270; ABE29573.1; -; Genomic_DNA.
DR AlphaFoldDB; Q143B6; -.
DR SMR; Q143B6; -.
DR STRING; 266265.Bxe_A3412; -.
DR EnsemblBacteria; ABE29573; ABE29573; Bxe_A3412.
DR KEGG; bxe:Bxe_A3412; -.
DR eggNOG; COG2352; Bacteria.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000001817; 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..994
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025554"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 646
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 994 AA; 109655 MW; 018ADC914C1D9199 CRC64;
MKAVRSDKTT QAATTAQAQK PAKAGSSKIK IVTAAPQAAN ASARQPASAQ APAPKANGRT
REDKDHPLFQ DIRYLGRLLG DVLREQEGDA VFDVVETIRQ TAVRFRREDD SAAAQTLDKK
LRSLSPEQTV SVVRAFSYFS HLANIAEDRH RNRRHRIHEL AGSTSQPGTI AHSLERLVEA
GAAATPVLQE FFNNALIVPV LTAHPTEVQR KSILDAQHDV ARLLAERDQQ LTDRERAHNE
AMLRARVTSL WQTRMLRDSR LSVADEIENA LSYYRATFLE EIPALYADIE EALAEHGLEA
RLPPFFQMGS WIGGDRDGNP NVTAETLENA ITRQAAVIFE HYMEQVHKLG AELSVSNLLA
GASDALKELA AVSPDQSPHR TDEPYRRALI GMYTRLAASA RVRLGEGSVP VRSAGRGAAP
VRAKPYADSA EFVRDLHVLI DSLAEHHGAP LAAPRLSPLA RAAEVFGFHL ASIDLRQSSD
VHEAVITELL RRAGVEENYA ELPEADKLNV LLSELAQPRP LRLPFAEYSD LVKSELGVLE
EARVTREKFG ARAVRNYIIS HTETVSDLVE VMLLQKETGL LRGCLGNAND PAQAGLMVIP
LFETIPDLRN APHIMRDLIA LPGVDALIEH QGNEQEVMLG YSDSNKDGGF LTSNWELYRA
ELALVSLFNE RGVTLRLFHG RGGTVGRGGG PTYQAILSQP PGTVDGQIRL TEQGEVIASK
FGNPEIGRRN LETVVAATLE ASLLPHGIAP AQLPAFEETM QQLSDAAMAS YRALVYETPG
FKEYFFESTP ISEIAELNIG SRPASRKLQD PKQRKIEDLR AIPWGFSWGQ CRLLLTGWYG
FGSAVAAHLD SAPSDAERTR RLALLKKMHK TWPFFANLLS NMDMVLAKTD LAVASRYAAL
VSDKKLRKHV FERIVAEWER TSKVLSEITG KSERLAENPL LARSIKNRFP YLDPLNHLQV
ELLKRHRAGD TNARVRRGIH LSINGIAAGL RNTG