ID Q3T9S7_MOUSE Unreviewed; 1179 AA. AC Q3T9S7; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 13-SEP-2023, entry version 116. DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594}; DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594}; GN Name=Pcx {ECO:0000313|MGI:MGI:97520}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE42943.1}; RN [1] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE42943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42943.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42943.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent CC carboxylation of the covalently attached biotin in the first step and CC the transfer of the carboxyl group to pyruvate in the second. CC {ECO:0000256|PIRNR:PIRNR001594}. 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 Evidence={ECO:0000256|PIRNR:PIRNR001594}; CC -!- COFACTOR: CC Name=biotin; Xref=ChEBI:CHEBI:57586; CC Evidence={ECO:0000256|ARBA:ARBA00001953, CC ECO:0000256|PIRNR:PIRNR001594}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|ARBA:ARBA00004742}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK172320; BAE42943.1; -; mRNA. DR AlphaFoldDB; Q3T9S7; -. DR SwissPalm; Q3T9S7; -. DR PeptideAtlas; Q3T9S7; -. DR AGR; MGI:97520; -. DR MGI; MGI:97520; Pcx. DR UniPathway; UPA00138; -. DR ChiTaRS; Pcx; mouse. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro. DR CDD; cd06850; biotinyl_domain; 1. DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 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 NCBIfam; TIGR01235; pyruv_carbox; 1. 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; 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; 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. DR PROSITE; PS50991; PYR_CT; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594}; KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594}; KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000256|ARBA:ARBA00023317}. FT DOMAIN 37..487 FT /note="Biotin carboxylation" FT /evidence="ECO:0000259|PROSITE:PS50979" FT DOMAIN 157..354 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 564..833 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50991" FT DOMAIN 1110..1179 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT ACT_SITE 329 FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1" FT BINDING 153 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 272 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 573 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 645 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 742 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /note="via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 772 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 774 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 909 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT MOD_RES 742 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4" FT MOD_RES 1145 FT /note="N6-biotinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4" SQ SEQUENCE 1179 AA; 129860 MW; 6B90E57D3F48C50F CRC64; MMLKFQTVRG GLRLLGVRRS SSAPVASPNV RRLEYKPIKR VMVANRGEIA IRVFRACTEL GIRTVAVYSE QDTGQMHRQK ADEAYLIGRG LAPVQAYLHI PDIIKVAKEN GVDAVHPGYG FLSERADFAQ ACQDAGVRFI GPSPEVVRKM GDKVEARAIA IAAGVPVVPG TDSPISSLHE AHEFSNTYGF PIIFKAAYGG GGRGMRVVHS YEELEENYTR AYSEALAAFG NGALFVEKFI EKPRHIEVQI LGDQYGNILH LYERDCSIQR RHQKVVEIAP ATHLDPQLRS RLTSDSVKLA KQVGYENAGT VEFLVDKHGK HYFIEVNSRL QVEHTVTEEI TDVDLVHAQI HVSEGRSLPD LGLRQENIRI NGCAIQCRVT TEDPARSFQP DTGRIEVFRS GEGMGIRLDN ASAFQGAVIS PHYDSLLVKV IAHGKDHPTA ATKMSRALAE FRVRGVKTNI PFLQNVLNNQ QFLAGTVDTQ FIDENPELFQ LRPAQNRAQK LLHYLGHVMV NGPTTPIPVN VSPSPVDPAV PVVPIGPPPA GFRDILLREG PEGFARAVRN HQGLLLMDTT FRDAHQSLLA TRVRTHDLKK IAPYVAHNFN KLFSMENWGG ATFDVAMRFL YECPWRRLQE LRELIPNIPF QMLLRGANAV GYTNYPDNVV FKFCEVAKEN GMDVFRVFDS LNYLPNMLLG MEAAGSAGGV VEAAISYTGD VADPSRTKYS LEYYMGLAEE LVRAGTHILC IKDMAGLLKP AACTMLVSSL RDRFPDLPLH IHTHDTSGAG VAAMLACAQA GADVVDVAVD SMSGMTSQPS MGALVACTKG TPLDTEVPLE RVFDYSEYWE GARGLYAAFD CTATMKSGNS DVYENEIPGG QYTNLHFQAH SMGLGSKFKE VKKAYVEANQ MLGDLIKVTP SSKIVGDLAQ FMVQNGLSRA EAEAQAEELS FPRSVVEFLQ GYIGIPHGGF PEPFRSKVLK DLPRIEGRPG ASLPPLNLKE LEKDLIDRHG EEVTPEDVLS AAMYPDVFAQ FKDFTATFGP LDSLNTRLFL QGPKIAEEFE VELERGKTLH IKALAVSDLN RAGQRQVFFE LNGQLRSILV KDTQAMKEMH FHPKALKDVK GQIGAPMPGK VIDIKVAAGD KVAKGQPLCV LSAMKMETVV TSPMEGTIRK VHVTKDMTLE GDDLILEIE //