GenomeNet

Database: UniProt
Entry: Q9HES8
LinkDB: Q9HES8
Original site: Q9HES8 
ID   PYC_ASPNG               Reviewed;        1192 AA.
AC   Q9HES8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   05-DEC-2018, entry version 98.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
GN   Name=pyc;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RA   Panneman H., Ruijter G.J.G., Van den Broeck H.C., Visser J.;
RT   "Aspergillus niger pyruvate carboxylase.";
RL   Submitted (JUL-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. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
DR   EMBL; AJ009972; CAC19838.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9HES8; -.
DR   SMR; Q9HES8; -.
DR   PRIDE; Q9HES8; -.
DR   eggNOG; ENOG410IU5D; Eukaryota.
DR   eggNOG; COG1038; LUCA.
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: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:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   ATP-binding; Biotin; Cytoplasm; Gluconeogenesis; Ligase;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW   Zinc.
FT   CHAIN         1   1192       Pyruvate carboxylase.
FT                                /FTId=PRO_0000146819.
FT   DOMAIN       40    492       Biotin carboxylation.
FT   DOMAIN      162    359       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      578    846       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1115   1190       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      586    590       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    334    334       {ECO:0000250}.
FT   METAL       587    587       Divalent metal cation. {ECO:0000250}.
FT   METAL       755    755       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       785    785       Divalent metal cation. {ECO:0000250}.
FT   METAL       787    787       Divalent metal cation. {ECO:0000250}.
FT   BINDING     158    158       ATP. {ECO:0000250}.
FT   BINDING     242    242       ATP. {ECO:0000250}.
FT   BINDING     277    277       ATP. {ECO:0000250}.
FT   BINDING     659    659       Substrate. {ECO:0000250}.
FT   BINDING     920    920       Substrate. {ECO:0000250}.
FT   MOD_RES     755    755       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1156   1156       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   1192 AA;  130866 MW;  C7630C689BA23A64 CRC64;
     MAAPRQPEEA VDDTEFIDDH HDQHRDSVHT RLRANSAIMQ FQKILVANRG EIPIRIFRTA
     HELSLQTVAV YSHEDHLSMH RQKADEAYMI GKRGQYTPVG AYLAIDEIVK IALEHGVHLI
     HPGYGFLSEN AEFARKVEQS GMVFVGPTPQ TIESLGDKVS ARQLAIRCDV PVVPGTPGPV
     ERYEEVKAFT DTYGFPIIIK AAFGGGGRGM RVVRDQAELR DSFERATSEA RSAFGNGTVF
     VERFLDRPKH IEVQLLGDNH GNVVHLFERD CSVQRRHQKV VEIAPAKDLP ADVRDRILAD
     AVKLAKSVNY RNAGTAEFLV DQQNRYYFIE INPRIQVEHT ITEEITGIDI VAAQIQIAAG
     ATLEQLGLTQ DRISTRGFAI QCRITTEDPS KGFSPDTGKI EVYRSAGGNG VRLDGGNGFA
     GAIITPHYDS MLVKCTCRGS TYEIARRKVV RALVEFRIRG VKTNIPFLTS LLSHPVFVDG
     TCWTTFIDDT PELFALVGSQ NRAQKLLAYL GDVAVNGSSI KGQIGEPKLK GDIIKPVLHD
     AAGKPLDVSV PATKGWKQIL DSEGPEAFAR AVRANKGCLI MDTTWRDAHQ SLLATRVRTI
     DLLNIAHETS HALANAYSLE CWGGATFDVA MRFLYEDPWD RLRKLRKAVP NIPFQMLLRG
     ANGVAYSSLP DNAIYHFCKQ AKKCGVDIFR VFDALNDVDQ LEVGIKAVHA AEGVVEATIC
     YSGDMLNPSK KYNLPYYLDL VDKVVQFKPH VLGIKDMAGV LKPQAARLLI GSIRERYPDL
     PIHVHTHDSA GTGVASMIAC AQAGADAVDA ATDSLSGMTS QPSIGAILAS LEGTEHDPGL
     NSAQVRALDT YWAQLRLLYS PFEAGLTGPD PEVYEHEIPG GQLTNLIFQA SQLGLGQQWA
     ETKKAYESAN DLLGDVVKVT PTSKVVGDLA QFMVSNKLTA EDVIARAGEL DFPGSVLEFL
     EGLMGQPYGG FPEPLRSRAL RDRRKLDKRP GLYLEPLDLA KIKSQIRENY GAATEYDVAS
     YAMYPKVFED YKKFVAKFGD LSVLPTRYFL AKPEIGEEFH VELEKGKVLI LKLLAIGPLS
     EQTGQREVFY EVNGEVRQVS VDDKKASVEN TARPKAELGD SSQVGAPMSG VVVEIRVHDG
     LEVKKGDPIA VLSAMKMEMV ISAPHSGKVS SLLVKEGDSV DGQDLVCKIV KA
//
DBGET integrated database retrieval system