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Entry: A0A1B9GC41_9TREE
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ID   A0A1B9GC41_9TREE        Unreviewed;      1209 AA.
AC   A0A1B9GC41;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   08-MAY-2019, entry version 15.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=I302_00069 {ECO:0000313|EMBL:OCF28581.1};
OS   Kwoniella bestiolae CBS 10118.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF28581.1, ECO:0000313|Proteomes:UP000092730};
RN   [1] {ECO:0000313|EMBL:OCF28581.1, ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF28581.1,
RC   ECO:0000313|Proteomes:UP000092730};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S.,
RA   Birren B.;
RT   "Evolution of pathogenesis and genome organization in the
RT   Tremellales.";
RL   Submitted (DEC-2013) 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; KI894018; OCF28581.1; -; Genomic_DNA.
DR   RefSeq; XP_019049651.1; XM_019186773.1.
DR   EnsemblFungi; OCF28581; OCF28581; I302_00069.
DR   GeneID; 30204468; -.
DR   EuPathDB; FungiDB:I302_00069; -.
DR   OrthoDB; 254436at2759; -.
DR   Proteomes; UP000092730; 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:UP000092730};
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:OCF28581.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092730}.
FT   DOMAIN       57    507       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      177    374       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      595    864       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1133   1208       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    349    349       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       604    604       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       773    773       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       803    803       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       805    805       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     173    173       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     257    257       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     292    292       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     676    676       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     938    938       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1209 AA;  132860 MW;  447143923AF3D1FF CRC64;
     MDKPSYFTHG RSTHQQIEAW VSHLGYDTSR PGTPSTPSVN PHTIHGLRKK QAGHSGPLKK
     VLVANRGEIA IRVFRTAHEL AMSTVAIYSH EDRMGAHRYK SDESYLVGKG LAPVAAYLSQ
     DDIVRIALEH EVDMIHPGYG FLSENAGFAK KVEDAGIAFI GPRPETIDAL GDKTKARTLA
     IKTGVPVVPG TPGPVESYDK ASEFIEKYGF PVIIKAAMGG GGRGMRVVRD QESFKESFER
     AVSEAKSAFG DGTVFIERFL DRPRHIEVQL LADGEGNCVH LFERDCSVQR RHQKVVEVAP
     APHLDESVRQ AILSDALKLA RGVNYRNAGT AEFLVDQQNR HYFIEINPRI QVEHTITEEI
     TGIDIVAAQI QIAAGVTLEQ LGLTQEHIHR RGFAIQCRIT TEDPAAGFQP DTGKIEVYRS
     AGGNGVRLDA SSGYAGAQIT PHYDSLLVKC SVSGATFEVA RRKMLRALIE FRIRGVKTNI
     PFLIRLLTHQ VFESGKTWTT FIDDTPDLFK LVHSQNRAQK LLAYLGDLAV NGSSIKGQMG
     EPGLNTEAII PQIRDNADSS KIVDTSVPCQ NGWRNIIVNE GPEAFAKAIR NYKGTLIMDT
     TWRDAHQSLL ATRMRTVDMA NIAKETSHAL QNAYSLECWG GATFDVSMRF LYEDPWDRLR
     TLRKLVPNIP LQALVRGANA VGYTSYPDNA IYDFSKKAVE AGLDIFRIFD SLNYLDNLKI
     GIDAAKKAGG VVEATICYSG DVANPKKTKY TLQYYLDLTD ALVKEGIHVL GIKDMAGLLK
     PEAARLLIGS IRKAHPDLPI HVHSHDTAGI AAASMIACAH AGADVVDVAI DDLSGLTSQP
     AMGAVCSALE QTGLGTGISH ENIQALNQYW SQIRKLYQCF EANVRASDSG VFDHEMPGGQ
     YTNLQFQASQ LGLGTQWLDI KRKYIEANQL CGDIVKVTPS SKVVGDFAQF MVSNNLSKDD
     VLDKASTLDF PSSVVEFFQG YLGQPYGGFP EPLRSNIIRD KERIDQRPGL SMKPLDFQTI
     KKELRDKFGL HITDFDVASY YMYPKVFEEF QGFVEKYGDL SVVPTRYFLG KPVIGEEMSI
     SIEQGKTLTI KLLAVGTLNE QKGTRECFFE LNGETRAVVI EDTNAAIEHV SREKASSDPG
     SIGSPMSGVV IDVRVKEGQE VKAGDPLCVL SAMKMESVVS SPVSGKVKRV LVKENDSIAQ
     GDLTVEITH
//
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