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 03-APR-2013, entry version 75.
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; Trichocomaceae;
OC mitosporic Trichocomaceae; 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 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: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; Hybrid_motif; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 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; PS50989; COA_CT_CTER; FALSE_NEG.
DR PROSITE; PS50980; COA_CT_NTER; FALSE_NEG.
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
//
