GenomeNet

Database: UniProt
Entry: Q29RK2
LinkDB: Q29RK2
Original site: Q29RK2 
ID   PYC_BOVIN               Reviewed;        1178 AA.
AC   Q29RK2; Q866R1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   10-APR-2019, entry version 109.
DE   RecName: Full=Pyruvate carboxylase, mitochondrial;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
DE   Flags: Precursor;
GN   Name=PC;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15248600; DOI=10.1081/ABIO-120037897;
RA   Agca C., Bidwell C.A., Donkin S.S.;
RT   "Cloning of bovine pyruvate carboxylase and 5' untranslated region
RT   variants.";
RL   Anim. Biotechnol. 15:47-66(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction,
CC       involving the ATP-dependent carboxylation of the covalently
CC       attached biotin in the first step and the transfer of the carboxyl
CC       group to pyruvate in the second. Catalyzes in a tissue specific
CC       manner, the initial reactions of glucose (liver, kidney) and lipid
CC       (adipose tissue, liver, brain) synthesis from pyruvate (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homotetramer. Interacts (via the biotin carboxylation
CC       domain) with SIRT4. {ECO:0000250|UniProtKB:P11498,
CC       ECO:0000250|UniProtKB:Q05920}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- PTM: Acetylation of Lys-748 might play a role in catalytic
CC       activity regulation. {ECO:0000250|UniProtKB:Q05920}.
DR   EMBL; AY185595; AAO27903.1; -; mRNA.
DR   EMBL; BC114135; AAI14136.1; -; mRNA.
DR   RefSeq; NP_808815.2; NM_177946.4.
DR   RefSeq; XP_005227045.1; XM_005226988.3.
DR   RefSeq; XP_005227046.1; XM_005226989.3.
DR   RefSeq; XP_005227047.1; XM_005226990.3.
DR   RefSeq; XP_005227048.1; XM_005226991.3.
DR   RefSeq; XP_005227049.1; XM_005226992.3.
DR   RefSeq; XP_005227050.1; XM_005226993.3.
DR   RefSeq; XP_005227051.1; XM_005226994.3.
DR   RefSeq; XP_015316738.1; XM_015461252.1.
DR   RefSeq; XP_015316739.1; XM_015461253.1.
DR   UniGene; Bt.10147; -.
DR   ProteinModelPortal; Q29RK2; -.
DR   SMR; Q29RK2; -.
DR   STRING; 9913.ENSBTAP00000030027; -.
DR   ChEMBL; CHEMBL1641351; -.
DR   PaxDb; Q29RK2; -.
DR   PeptideAtlas; Q29RK2; -.
DR   PRIDE; Q29RK2; -.
DR   Ensembl; ENSBTAT00000026258; ENSBTAP00000026258; ENSBTAG00000019700.
DR   Ensembl; ENSBTAT00000030039; ENSBTAP00000030027; ENSBTAG00000019700.
DR   Ensembl; ENSBTAT00000068219; ENSBTAP00000058830; ENSBTAG00000019700.
DR   Ensembl; ENSBTAT00000081699; ENSBTAP00000067685; ENSBTAG00000019700.
DR   Ensembl; ENSBTAT00000086901; ENSBTAP00000069242; ENSBTAG00000019700.
DR   GeneID; 338471; -.
DR   KEGG; bta:338471; -.
DR   CTD; 5091; -.
DR   VGNC; VGNC:56274; PC.
DR   eggNOG; ENOG410IU5D; Eukaryota.
DR   eggNOG; COG1038; LUCA.
DR   GeneTree; ENSGT00900000141164; -.
DR   HOGENOM; HOG000282801; -.
DR   HOVERGEN; HBG008340; -.
DR   InParanoid; Q29RK2; -.
DR   KO; K01958; -.
DR   OMA; GQPHGGF; -.
DR   OrthoDB; 254436at2759; -.
DR   TreeFam; TF300535; -.
DR   BRENDA; 6.4.1.1; 908.
DR   Reactome; R-BTA-196780; Biotin transport and metabolism.
DR   Reactome; R-BTA-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:Q29RK2; -.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000019700; Expressed in 9 organ(s), highest expression level in adult mammalian kidney.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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   Acetylation; ATP-binding; Biotin; Complete proteome; Gluconeogenesis;
KW   Ligase; Lipid biosynthesis; Lipid metabolism; Manganese;
KW   Metal-binding; Mitochondrion; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Pyruvate; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     20       Mitochondrion. {ECO:0000255}.
FT   CHAIN        21   1178       Pyruvate carboxylase, mitochondrial.
FT                                /FTId=PRO_0000239868.
FT   DOMAIN       36    486       Biotin carboxylation.
FT   DOMAIN      156    353       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      563    832       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1109   1178       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      571    575       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    328    328       {ECO:0000250}.
FT   METAL       572    572       Manganese. {ECO:0000250}.
FT   METAL       741    741       Manganese; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       771    771       Manganese. {ECO:0000250}.
FT   METAL       773    773       Manganese. {ECO:0000250}.
FT   BINDING     152    152       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
FT   BINDING     271    271       ATP. {ECO:0000250}.
FT   BINDING     644    644       Substrate. {ECO:0000250}.
FT   BINDING     908    908       Substrate. {ECO:0000250}.
FT   MOD_RES      35     35       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES      39     39       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES      79     79       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES      79     79       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     148    148       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     152    152       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     241    241       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     297    297       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     319    319       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     434    434       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     442    442       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     589    589       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     661    661       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     717    717       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     741    741       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES     748    748       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     892    892       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     969    969       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES     992    992       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES    1003   1003       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P52873}.
FT   MOD_RES    1061   1061       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES    1090   1090       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   MOD_RES    1124   1124       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q05920}.
FT   MOD_RES    1144   1144       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT    149    149       M -> I (in Ref. 1; AAO27903).
FT                                {ECO:0000305}.
FT   CONFLICT    157    157       A -> T (in Ref. 1; AAO27903).
FT                                {ECO:0000305}.
FT   CONFLICT    163    163       G -> D (in Ref. 1; AAO27903).
FT                                {ECO:0000305}.
FT   CONFLICT    171    171       D -> N (in Ref. 1; AAO27903).
FT                                {ECO:0000305}.
FT   CONFLICT    439    439       A -> D (in Ref. 1; AAO27903).
FT                                {ECO:0000305}.
FT   CONFLICT    568    568       T -> A (in Ref. 2; AAI14136).
FT                                {ECO:0000305}.
FT   CONFLICT    592    592       P -> L (in Ref. 2; AAI14136).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1178 AA;  129698 MW;  15DDD18BC7920D01 CRC64;
     MLKFQTVRGS LRLLAIRRTS TATAASPNVR RLEYKPIKKV MVANRGEIAI RVFRACTELG
     IRTVAVYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP DIIKVAKENN VDAVHPGYGF
     LSERADFAQA CQDAGVRFIG PSPEVVRKMG DKVEARAIAI AAGVPVVPGT DAPITSLHEA
     HEFSNTYGFP IIFKAAYGGG GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE
     KPRHIEVQIL GDQYGNILHL YERDCSIQRR HQKVVEIAPA AHLDPQLRTR LTSDSVKLAK
     QVGYENAGTV EFLVDRHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH VAEGRSLPDL
     GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG EGMGIRLDNA SAFQGAVISP
     HYDSLLVKVI AHGKDHPTAA TKMSRALAEF RVRGVKTNIP FLQNVLNNQQ FLAGTVDTQF
     IDENPELFQL RPAQNRAQKL LHYLGHVMVN GPTTPIPVKA SPSPTDPIVP VVPIGPPPTG
     FRDILLREGP EGFARAVRNH EGLLLMDTTF RDAHQSLLAT RVRTHDLKKI SPYVAHSFNK
     LFSIENWGGA TFDVAMRFLY ECPWRRLQEL RELVPNIPFQ MLLRGANAVG YTNYPDNVVF
     KFCEVAKENG MDIFRVFDSL NYLPNLLLGM EAAGSAGGVV EAAISYTGDV SDPSRTKYSL
     QYYMGLAEEL VRAGTHILCI KDMAGLLKPT ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV
     AAMLACAHAG ADVVDVAADS MSGMTSQPSM GALVACTRGT PLDTGVPLER VFDYSEYWEG
     ARGLYAAFDC TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM
     LGDLIKVTPS SKIVGDLAQF MVQNGLTRAE AEAQAEELSF PRSVVEFLQG YIGIPHGGFP
     EPLRSKVLKD LPRVEGRPGA SLPPLDLQAL EKELTERHGE EVTPEDVLSA AMYPDVFAHF
     KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV ELERGKTLHI KALAISDLNR AGQRQVFFEL
     NGQLRSILVK DTQAMKEMHF HPKALKDVKG QIGAPMPGKV IDIKVAAGAK VTKGQPLCVL
     SAMKMETVVT SPVEGTVRKV HVTKDMTLEG DDLILEIE
//
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