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Database: UniProt
Entry: O93918
LinkDB: O93918
Original site: O93918 
ID   PYC_ASPTE               Reviewed;        1193 AA.
AC   O93918;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   19-FEB-2014, entry version 79.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
GN   Name=pyc;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li Y.F., Chen M.C., Lin Y.H., Hsu C.C., Tsai Y.C.;
RT   "Cloning and sequencing of the cDNA encoding pyruvate carboxylase from
RT   Aspergillus terreus.";
RL   Submitted (OCT-1998) 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate.
CC   -!- COFACTOR: Biotin (By similarity).
CC   -!- COFACTOR: Zinc (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC   -!- SIMILARITY: Contains 1 biotinyl-binding domain.
CC   -!- SIMILARITY: Contains 1 carboxyltransferase domain.
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DR   EMBL; AF097728; AAC69197.1; -; mRNA.
DR   ProteinModelPortal; O93918; -.
DR   SMR; O93918; 41-496, 501-1190.
DR   STRING; 33178.CADATEAP00005485; -.
DR   PRIDE; O93918; -.
DR   eggNOG; COG1038; -.
DR   BioCyc; MetaCyc:MONOMER-13631; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   ATP-binding; Biotin; Cytoplasm; Gluconeogenesis; Ligase;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW   Zinc.
FT   CHAIN         1   1193       Pyruvate carboxylase.
FT                                /FTId=PRO_0000146820.
FT   DOMAIN       41    493       Biotin carboxylation.
FT   DOMAIN      163    360       ATP-grasp.
FT   DOMAIN      579    847       Carboxyltransferase.
FT   DOMAIN     1123   1190       Biotinyl-binding.
FT   REGION      587    591       Substrate binding (By similarity).
FT   ACT_SITE    335    335       By similarity.
FT   METAL       588    588       Divalent metal cation (By similarity).
FT   METAL       756    756       Divalent metal cation; via carbamate
FT                                group (By similarity).
FT   METAL       786    786       Divalent metal cation (By similarity).
FT   METAL       788    788       Divalent metal cation (By similarity).
FT   BINDING     159    159       ATP (By similarity).
FT   BINDING     243    243       ATP (By similarity).
FT   BINDING     278    278       ATP (By similarity).
FT   BINDING     660    660       Substrate (By similarity).
FT   BINDING     921    921       Substrate (By similarity).
FT   MOD_RES     756    756       N6-carboxylysine (By similarity).
FT   MOD_RES    1157   1157       N6-biotinyllysine (By similarity).
SQ   SEQUENCE   1193 AA;  131222 MW;  6E24E000CE793206 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 TPELFALVGS QNRAQKLLAY LGDVAVNGSS IKGQMGEPKF KGEIIKPKLL
     DAQGKPLDVS QPCTKGWKQI IDQEGPVAFA KAVRANKGCL IMDTTWRDAH QSLLATRVRT
     IDLLNIAHET SHALSNAYSL ECWGGATFDV AMRFLYEDPW DRLRKMRKAV PNIPFQMLLR
     GANGVAYSSL PDNAIYHFCK NAKKCGVDIF RVFDALNDID QLEVGIKAVH AAEGVVEATV
     CYSGDMLNPK KKYNLEYYLA LVDKIVALKP HVLGIKDMAG VLKPQAARLL VGSIRERYPD
     LPIHVHTHDS AGTGVASMIA CAQAGADAVD AATDSMSGMT SQPSIGAILA SLEGTEHDPG
     LNSAHVRALD SYWAQLRLLY SPFEANLTGP DPEVYEHEIP GGQLTNLIFQ ASQLGLGQQW
     AETKKAYEVA NDLLGDIVKV TPTSKVVGDL AQFIVSNKLS AQDVVDRAAE LDFPGSVLEF
     LEGLMGQPFG GFPEPLRSRA LRNRRKLDKR PGLYLEPLDL AAIKNQIREQ FGSATEYDVA
     SYAMYPKVFE DYKKFVQKYG DLSVLPTRYF LAKPEIGEEF HVELEKGKVL ILKLLAIGPL
     SEQTGQREVF YEVNGEVRQV SIDDKKASID NTARPKADVG DSSQVGAPMS GVVVEIRVHD
     GLEVKKGDPL AVLSAMKMEM VISAPHSGKV SGLLVKEGDS VDGQDLVCKI TKA
//
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