ID G1R362_NOMLE Unreviewed; 1094 AA.
AC G1R362;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|Ensembl:ENSNLEP00000007634.2};
GN Name=PC {ECO:0000313|Ensembl:ENSNLEP00000007634.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000007634.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000007634.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000007634.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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DR EMBL; ADFV01079804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01079805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01079806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01079807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01079808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01079809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000007634; -.
DR Ensembl; ENSNLET00000008003.3; ENSNLEP00000007634.2; ENSNLEG00000006274.3.
DR eggNOG; KOG0369; Eukaryota.
DR GeneTree; ENSGT00900000141164; -.
DR HOGENOM; CLU_000395_1_0_1; -.
DR InParanoid; G1R362; -.
DR TreeFam; TF300535; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001073; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR GO; GO:0006739; P:NADP metabolic process; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0044794; P:positive regulation by host of viral process; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR GO; GO:0019074; P:viral RNA genome packaging; IEA:Ensembl.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
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; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 3.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR001594-
KW 2}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR001594-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073}.
FT DOMAIN 36..473
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 147..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1025..1094
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 707..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 559
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 631
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 722
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 824
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
SQ SEQUENCE 1094 AA; 120815 MW; D8C0020C5E3B9B34 CRC64;
MLKFRTVHGG LRLLGIRRTS TAPAASPNVR RLEYKPIKKV MVANRGEIAI RVFRACTELG
IRTVAIYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP DIIKVAKNNV DAVHPADFAX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXSLPTGVP VVLAQMPPSL LQHYGFPIIF
KAAYGGGGRG MRVVHSYEEL EENYTRAYSE ALAAFGNGAL FVEKFIEKPR HIEVQILGDQ
YGNILHLYER DCSIQRRHQK VVEIAPAAHL DPQLRTRLTS DSVKLAKQVG YENAGTVEFL
VDRHGKHYFI EVNSRLQVEH TVTEEITDVD LVHAQIHVAE GRSLPDLGLR QENIRINGCA
IQCRVTTEDP ARSFQPDTGR IEVFRSGEGM GIRLDNASAF QGAVISPHYD SLLVKVIAHG
KDHPTAATKM SRALAEFRVR GVKTNIAFLQ NVLNNQQFLA GTVDTQFIDE NPELFQLRPA
QNRAQKLLHY LGHVMVNGPT TPIPVKASPS PTDPIVPAVP IGPPPAGFRD ILLREGPEGF
ARAVRNHPGL LLMDTTFRDA HQSLLATRVR THDLKKIAPY VAHNFSKLFS MENWGGATFD
VAMRFLYECP WRRLQELREL IPNIPFQMLL RGANAVGYTN YPDNVVFKHY LVWPRGRGCC
LEIIEKRRIG VAEADRLLNY SLTPGAAEGL RLASGLLAQC PLPQPVTGLA DPPGPGPHLC
GHPSPVDATS PASSGSGLPA EVPMERVFDY SEYWEGARGL YAAFDCTATM KSGNSDVYEN
EIPGGQYTNL HFQAHSMGLG SKFKEVKKAY VEANQMLGDL IKVTPSSKIV GDLAQFMVQN
GLSRAEAEAQ AEELSFPRSV VEFLQGYIGV PHGGFPEPFR SKVLKDLPRV EGRPGASLPP
LDLQALEKEL VDRHGEEVTP EDVLSAAMYP DVFAHFKDFT ATFGPLDSLN TRLFLQGPKI
AEEFEVELER GKTLHIKALA VSDLNRAGQR QVFFELNGQL RSILVKDTQA MKEMHFHPKA
LKDVKGQIGA PMPGKVIDIK VAAGAKVAKG QPLCVLSAMK METVVTSPME GTVRKVHVTK
DMTLEGDDLI LEIE
//
