| Tag | Content |
|---|
| CPLM ID | CPLM-011326 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Pyruvate carboxylase, mitochondrial |
Protein Synonyms/Alias | Pyruvic carboxylase; PCB |
Gene Name | Pc |
Gene Synonyms/Alias | Pcx |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 316 | TVEFLVDKHGKHYFI | acetylation | [1] |
|
Reference | [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y. Mol Cell. 2006 Aug;23(4):607-18. [ PMID: 16916647] |
Functional Description | Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate. |
Sequence Annotation | DOMAIN 36 486 Biotin carboxylation.
DOMAIN 156 353 ATP-grasp.
DOMAIN 563 832 Carboxyltransferase.
DOMAIN 1110 1177 Biotinyl-binding.
REGION 571 575 Substrate binding (By similarity).
ACT_SITE 328 328 By similarity.
METAL 572 572 Manganese (By similarity).
METAL 741 741 Manganese; via carbamate group (By
METAL 771 771 Manganese (By similarity).
METAL 773 773 Manganese (By similarity).
BINDING 152 152 ATP (By similarity).
BINDING 236 236 ATP (By similarity).
BINDING 271 271 ATP (By similarity).
BINDING 644 644 Substrate (By similarity).
BINDING 908 908 Substrate (By similarity).
MOD_RES 316 316 N6-acetyllysine.
MOD_RES 741 741 N6-carboxylysine (By similarity).
MOD_RES 1090 1090 N6-acetyllysine (By similarity).
MOD_RES 1144 1144 N6-biotinyllysine (By similarity). |
Keyword | Acetylation; ATP-binding; Biotin; Complete proteome; Gluconeogenesis; Ligase; Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding; Mitochondrion; Multifunctional enzyme; Nucleotide-binding; Pyruvate; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1178 AA |
Protein Sequence | MLKFQTVRGG LRLLGVRRSS SAPVASPNVR RLEYKPIKKV MVANRGEIAI RVFRACTELG 60
IRTVAVYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP DIIKVAKENG VDAVHPGYGF 120
LSERADFAQA CQDAGVRFIG PSPEVVRKMG DKVEARAIAI AAGVPVVPGT DSPISSLHEA 180
HEFSNTFGFP IIFKAAYGGG GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE 240
KPRHIEVQIL GDQYGNILHL YERDCSIQRR HQKVVEIAPA THLDPQLRSR LTSDSVKLAK 300
QVGYENAGTV EFLVDKHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH VSEGRSLPDL 360
GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG EGMGIRLDNA SAFQGAVISP 420
HYDSLLVKVI AHGKDHPTAA TKMSRALAEF RVRGVKTNIP FLQNVLNNQQ FLAGTVDTQF 480
IDENPELFQL RPAQNRAQKL LHYLGHVMVN GPTTPIPVNV SPSPVDPAVP VVPIGPPPAG 540
FRDILLREGP EGFARAVRNH QGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFNK 600
LFSMENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG YTNYPDNVVF 660
KFCEVAKENG MDVFRVFDSL NYLPNMLLGM EAAGSAGGVV EAAISYTGDV ADPSRTKYSL 720
EYYMGLAEEL VRAGTHILCI KDMAGLLKPA ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV 780
AAMLACAQAG ADVVDVAVDS MSGMTSQPSM GALVACTKGT PLDTEVPLER VFDYSEYWEG 840
ARGLYAAFDC TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM 900
LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG YIGIPHGGFP 960
EPFRSKVLKD LPRIEGRPGA SLPPLNLKEL EKDLIDRHGE EVTPEDVLSA AMYPDVFAQF 1020
KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV ELERGKTLHI KALAVSDLNR AGQRQVFFEL 1080
NGQLRSILVK DTQAMKEMHF HPKALKDVKG QIGAPMPGKV IDIKVAAGDK VAKGQPLCVL 1140
SAMKMETVVT SPMEGTIRKV HVTKDMTLEG DDLILEIE 1178 |
Gene Ontology | GO:0005743; C:mitochondrial inner membrane; IDA:MGI. GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004075; F:biotin carboxylase activity; IEA:InterPro. GO:0003677; F:DNA binding; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004736; F:pyruvate carboxylase activity; IEA:EC. GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |