PYC_ASPTN
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 03-AUG-2022, entry version 80.
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;
OC Aspergillus subgen. Circumdati.
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., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA 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, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU34502.1; Type=Frameshift; 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 AlphaFoldDB; Q0CLK1; -.
DR SMR; Q0CLK1; -.
DR STRING; 341663.Q0CLK1; -.
DR PRIDE; Q0CLK1; -.
DR GeneID; 4320946; -.
DR eggNOG; KOG0369; Eukaryota.
DR OrthoDB; 254436at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; Reference proteome;
KW Zinc.
FT CHAIN 1..1193
FT /note="Pyruvate carboxylase"
FT /id="PRO_0000283709"
FT DOMAIN 41..493
FT /note="Biotin carboxylation"
FT DOMAIN 163..360
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 579..847
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 1116..1191
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 335
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 587..591
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 756
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 786
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 788
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 921
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 756
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1157
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
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
