PYC_ASPNG
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 03-AUG-2022, entry version 109.
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;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
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, involving
CC the ATP-dependent carboxylation of the covalently attached biotin in
CC the first step and the transfer of the carboxyl group to pyruvate in
CC the second. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, 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}.
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DR EMBL; AJ009972; CAC19838.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HES8; -.
DR SMR; Q9HES8; -.
DR STRING; 5061.CADANGAP00003832; -.
DR PRIDE; Q9HES8; -.
DR VEuPathDB; FungiDB:An04g02090; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1031996; -.
DR VEuPathDB; FungiDB:ATCC64974_78120; -.
DR VEuPathDB; FungiDB:M747DRAFT_295217; -.
DR eggNOG; KOG0369; Eukaryota.
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: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; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Pyruvate; Zinc.
FT CHAIN 1..1192
FT /note="Pyruvate carboxylase"
FT /id="PRO_0000146819"
FT DOMAIN 40..492
FT /note="Biotin carboxylation"
FT DOMAIN 162..359
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 578..846
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 1115..1190
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 586..590
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 659
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 755
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 785
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 787
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 920
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 755
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1156
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT 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
