ID   Q3T9S7_MOUSE            Unreviewed;      1179 AA.
AC   Q3T9S7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   07-OCT-2020, entry version 107.
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|ARBA:ARBA00000564,
CC         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}.
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DR   EMBL; AK172320; BAE42943.1; -; mRNA.
DR   SwissPalm; Q3T9S7; -.
DR   PeptideAtlas; Q3T9S7; -.
DR   PRIDE; Q3T9S7; -.
DR   MGI; MGI:97520; Pcx.
DR   UniPathway; UPA00138; -.
DR   ChiTaRS; Pcx; mouse.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; PS50991; PYR_CT; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-ProRule:PRU00409};
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   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|PIRSR:PIRSR001594-2,
KW   ECO:0000256|PROSITE-ProRule:PRU00409};
KW   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   METAL           573
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   METAL           742
FT                   /note="Divalent metal cation; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   METAL           772
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   METAL           774
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         153
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         237
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         272
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         645
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         909
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
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
//