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Database: UniProt
Entry: Q0CLK1
LinkDB: Q0CLK1
Original site: Q0CLK1 
ID   PYC_ASPTN               Reviewed;        1193 AA.
AC   Q0CLK1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   29-OCT-2014, entry version 47.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
GN   Name=pyc; ORFNames=ATEG_05433;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction,
CC       involving the ATP-dependent carboxylation of the covalently
CC       attached biotin in the first step and the transfer of the carboxyl
CC       group to pyruvate in the second. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate.
CC   -!- COFACTOR: Biotin. {ECO:0000250}.
CC   -!- COFACTOR: Zinc. {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00409}.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 biotinyl-binding domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 carboxyltransferase domain. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU34502.1; Type=Frameshift; Positions=260, 263, 503; Evidence={ECO:0000305};
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DR   EMBL; CH476600; EAU34502.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_001214611.1; XM_001214611.1.
DR   ProteinModelPortal; Q0CLK1; -.
DR   SMR; Q0CLK1; 41-496, 501-1190.
DR   GeneID; 4320946; -.
DR   OrthoDB; EOG7GQZ41; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA 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:UniProtKB-UniPathway.
DR   Gene3D; 1.10.10.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866:SF10; PTHR18866:SF10; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00289; CPSase_L_chain; 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   3: Inferred from homology;
KW   ATP-binding; Biotin; Complete proteome; Cytoplasm; Gluconeogenesis;
KW   Ligase; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Pyruvate; Reference proteome; Zinc.
FT   CHAIN         1   1193       Pyruvate carboxylase.
FT                                /FTId=PRO_0000283709.
FT   DOMAIN       41    493       Biotin carboxylation.
FT   DOMAIN      163    360       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      579    847       Carboxyltransferase.
FT   DOMAIN     1123   1190       Biotinyl-binding.
FT   REGION      587    591       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    335    335       {ECO:0000250}.
FT   METAL       588    588       Divalent metal cation. {ECO:0000250}.
FT   METAL       756    756       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       786    786       Divalent metal cation. {ECO:0000250}.
FT   METAL       788    788       Divalent metal cation. {ECO:0000250}.
FT   BINDING     159    159       ATP. {ECO:0000250}.
FT   BINDING     243    243       ATP. {ECO:0000250}.
FT   BINDING     278    278       ATP. {ECO:0000250}.
FT   BINDING     660    660       Substrate. {ECO:0000250}.
FT   BINDING     921    921       Substrate. {ECO:0000250}.
FT   MOD_RES     756    756       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1157   1157       N6-biotinyllysine. {ECO:0000250}.
SQ   SEQUENCE   1193 AA;  131267 MW;  3E870019336E4B68 CRC64;
     MAAPYRQPEE AVDDSEFIDD HHDHLRDTVH HRLRANSAIM QFQKILVANR GEIPIRIFRT
     AHELSLQTVA IFSHEDRLSM HRQKADEAYM IGHRGQYTPV GAYLAADEIV KIALEHGVHL
     IHPGYGFLSE NADFARKVEK AGMVFVGPTP DTIDSLGDKV SARQLAIRCN VPVVPGTEGP
     VERYEEVKAF TDTYGFPIII KAAFGGGGRG MRVVRNQADL RDSFERATSE ARSAFGNGTV
     FVERFLDKPK HIEVQLLGDN HGNVVHLFER DCSVQRRHQK VVEVAPAKDL PTDVRDRILS
     DAVKLAKSVN YRNAGTAEFL VDQQNRHYFI EINPRIQVEH TITEEITGID IVAAQIQIAA
     GATLEQLGLT QDRISTRGFA IQCRITTEDP SKGFSPDTGK IEVYRSAGGN GVRLDGGNGF
     AGAIITPHYD SMLVKCTCRG STYEIARRKV VRALVEFRIR GVKTNIPFLT SLLSHPTFVD
     GNCWTTFIDD TTELFALVGS QNRAQKLLAY LGDVAVNGSS IKGQMGEPKF KGEIIKPKLL
     DAQGKPLDVS HPCTKGWKQI IDQEGPVAFA KAVRANKGCL IMDTTWRDAH QSLLATRVRT
     IDLLNIAHET SHALSNAYSL ECWGGATFDV AMRFLYEDPW DRLRKMRKAV PNIPFQMLLR
     GANGVAYSSL PDNAIYHFCK NAKKCGVDIF RVFDALNDVD QLEVGIKAVH AAEGVVEATV
     CYSGDMLNPK KKYNLEYYLA LVDKIVALKP HVLGIKDMAG VLKPQAARLL VGSIRERYPD
     LPIHVHTHDS AGTGVASMIA CAQAGADAVD AATDSMSGMT SQPSIGAILA SLEGTEHDPG
     LNSAHVRALD SYWAQLRLLY SPFEANLTGP DPEVYEHEIP GGQLTNLIFQ ASQLGLGQQW
     AETKKAYEVA NDLLGDIVKV TPTSKVVGDL AQFIVSNKLS AQDVIDRAAE LDFPGSVLEF
     LEGLMGQPFG GFPEPLRSRA LRNRRKLDKR PGLYLEPLDL AAIKNQIREQ FGSATEYDVA
     SYAMYPKVFE DYKKFVQKYG DLSVLPTRYF LAKPEIGEEF HVELEKGKML ILKLLAIGPL
     SEQTGQREVF YEVNGEVRQV SIDDKKASID NTARPKADVG DSSQVGAPMS GVVVEIRVHD
     GLEVKKGDPL AVLSAMKMEM VISAPHSGKV SGLLVKEGDS VDGQDLVCKI TKA
//
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