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Database: UniProt
Entry: L8G0F2_PSED2
LinkDB: L8G0F2_PSED2
Original site: L8G0F2_PSED2 
ID   L8G0F2_PSED2            Unreviewed;      1189 AA.
AC   L8G0F2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   05-JUN-2019, entry version 42.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=GMDG_02049 {ECO:0000313|EMBL:ELR06254.1};
OS   Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS   white-nose syndrome fungus) (Geomyces destructans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR06254.1, ECO:0000313|Proteomes:UP000011064};
RN   [1] {ECO:0000313|Proteomes:UP000011064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Geomyces destructans 20631-21.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELR06254.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=20631-21 {ECO:0000313|EMBL:ELR06254.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Geomyces destructans 20631-21.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step
CC       and the transfer of the carboxyl group to pyruvate in the second.
CC       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594,
CC         ECO:0000256|SAAS:SAAS00197451};
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DR   EMBL; GL573195; ELR06254.1; -; Genomic_DNA.
DR   EMBL; GL573195; ELR06255.1; -; Genomic_DNA.
DR   RefSeq; XP_012740452.1; XM_012884998.1.
DR   RefSeq; XP_012740453.1; XM_012884999.1.
DR   EnsemblFungi; ELR06254; ELR06254; GMDG_02049.
DR   EnsemblFungi; ELR06255; ELR06255; GMDG_02049.
DR   OrthoDB; 254436at2759; -.
DR   Proteomes; UP000011064; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234148};
KW   Biotin {ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|SAAS:SAAS00296904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011064};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|SAAS:SAAS00232059};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234082};
KW   Pyruvate {ECO:0000313|EMBL:ELR06254.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011064}.
FT   DOMAIN       37    489       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      159    356       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      575    843       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1112   1187       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   REGION        1     23       Disordered. {ECO:0000256|MobiDB-lite:
FT                                L8G0F2}.
FT   ACT_SITE    331    331       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       584    584       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       752    752       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       782    782       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       784    784       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     155    155       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     239    239       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     274    274       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     656    656       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     917    917       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1189 AA;  130437 MW;  037BFCF9E08A105D CRC64;
     MSAGDPNGAA NEVFEESGDE RQSQSIQHIR ANSSIMQLKK ILVANRGEIP IRIFRTAHEL
     SLQTVAVFSY EDRLSMHRQK ADEAYVIGKR GQYTPVGAYL AGDEIIKIAL QHGVNMIHPG
     YGFLSENAEF ARNVEKAGLV FVGPSPEVID ALGDKVSART LAIKAGVPVV PGTEGAVEKF
     EDVKKFTDEY GFPIIIKAAY GGGGRGMRVV REQASLKESF DRATSEAKSA FGNGTVFVER
     FLDRPKHIEV QLLGDNHGNI VHLYERDCSV QRRHQKVVEL APAKDLPQSV REALLNDAVK
     LAKSVNYRNA GTAEFLVDQQ NRYYFIEINP RIQVEHTITE EITGIDIIAA QIQIAAGATL
     PQLGLTQDRI STRGFAIQCR ITTEDPSKQF SPDTGKIEVY RSAGGNGVRL DGGNGFAGAV
     ITPYYDSMLV KCTCHGSTYE IVRRKMLRAL VEFRIRGVKT NIPFLASLLT HPTFIDGNCW
     TTFIDDTPEL FDLVGSQNRA QKLLAYLGDI AVNGSSIKGQ VGEPKFKGEI IMPELFDDEG
     TKIDVTEPST QGWRQILIEQ GPEAFAKSVR ANKGCLLMDT TWRDAHQSLL ATRVRTVDLL
     NIAKETSHAY ANLYSLECWG GATFDVAMRF LYEDPWDRLR KMRKLIPNIP FQMLLRGANG
     VAYSSLPDNA IYHFVEQAKK NGVDIFRVFD ALNDIDQLEL GIKAVHKAGG VVEGTVCYSG
     DMLNPKKKYN LEYYLDVVAK LVALNIHVLG IKDMAGVLKP KAATLLIGAI REKYPDLPIH
     VHTHDSAGTG VASMAACAAA GADVVDTATD SLSGMTSQPS VGAVLSSLEG SDFETGLNVH
     HIRAIDTYWA QLRLLYSPFE AHLTGPDPEV YEHEIPGGQL TNMMFQAQQL GLGAQWAQTK
     KAYEQANDVL GDVIKVTPVS KTVGDLAQFM VSNKLTPEAL IAKASELDFP GSVLDFFEGL
     MGQPYGGFPE PLRSHALRDR RKLDKRPGLF LPPIDFAKVK KEIRQKWGSV TECDIASSVM
     YPAVFNDYKK FTEKYGDLSV LPTKYFLSKP EIGEEFSVEL EKGKVLILKL LAIGPLSDIT
     GQRDVFYEMN GEVRSITVDD KLAAVENVSR PKADPGDSSQ CGSPMAGVVV EIRVKEGSEV
     KKGDVIAVIS AMKMEMVVTA AHNGVIAQLV VKEGDSLSGQ DLICRVVKP
//
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