CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003881
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate carboxylase 1 
Protein Synonyms/Alias
 Pyruvic carboxylase 1; PCB 1 
Gene Name
 PYC1 
Gene Synonyms/Alias
 PYV; YGL062W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
21NLLGEKNKILVANRGubiquitination[1]
257SVQRRHQKVVEVAPAubiquitination[1]
265VVEVAPAKTLPREVRubiquitination[1]
542WRQVLLEKGPAEFARacetylation[2]
661DHFVKQAKDNGVDIFubiquitination[1]
741KDMAGTMKPAAAKLLubiquitination[1]
902VKVTPTSKVVGDLAQubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
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. 
Sequence Annotation
 DOMAIN 18 470 Biotin carboxylation.
 DOMAIN 140 337 ATP-grasp.
 DOMAIN 557 824 Carboxyltransferase.
 DOMAIN 1101 1168 Biotinyl-binding.
 REGION 565 569 Substrate binding (By similarity).
 ACT_SITE 312 312 By similarity.
 METAL 566 566 Divalent metal cation (By similarity).
 METAL 734 734 Divalent metal cation; via carbamate
 METAL 764 764 Divalent metal cation (By similarity).
 METAL 766 766 Divalent metal cation (By similarity).
 BINDING 136 136 ATP (By similarity).
 BINDING 220 220 ATP (By similarity).
 BINDING 255 255 ATP (By similarity).
 BINDING 638 638 Substrate (By similarity).
 BINDING 898 898 Substrate (By similarity).
 MOD_RES 734 734 N6-carboxylysine (By similarity).
 MOD_RES 1135 1135 N6-biotinyllysine.  
Keyword
 ATP-binding; Biotin; Complete proteome; Cytoplasm; Direct protein sequencing; Gluconeogenesis; Ligase; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1178 AA 
Protein Sequence
MSQRKFAGLR DNFNLLGEKN KILVANRGEI PIRIFRTAHE LSMQTVAIYS HEDRLSTHKQ 60
KADEAYVIGE VGQYTPVGAY LAIDEIISIA QKHQVDFIHP GYGFLSENSE FADKVVKAGI 120
TWIGPPAEVI DSVGDKVSAR NLAAKANVPT VPGTPGPIET VEEALDFVNE YGYPVIIKAA 180
FGGGGRGMRV VREGDDVADA FQRATSEART AFGNGTCFVE RFLDKPKHIE VQLLADNHGN 240
VVHLFERDCS VQRRHQKVVE VAPAKTLPRE VRDAILTDAV KLAKECGYRN AGTAEFLVDN 300
QNRHYFIEIN PRIQVEHTIT EEITGIDIVA AQIQIAAGAS LPQLGLFQDK ITTRGFAIQC 360
RITTEDPAKN FQPDTGRIEV YRSAGGNGVR LDGGNAYAGT IISPHYDSML VKCSCSGSTY 420
EIVRRKMIRA LIEFRIRGVK TNIPFLLTLL TNPVFIEGTY WTTFIDDTPQ LFQMVSSQNR 480
AQKLLHYLAD VAVNGSSIKG QIGLPKLKSN PSVPHLHDAQ GNVINVTKSA PPSGWRQVLL 540
EKGPAEFARQ VRQFNGTLLM DTTWRDAHQS LLATRVRTHD LATIAPTTAH ALAGRFALEC 600
WGGATFDVAM RFLHEDPWER LRKLRSLVPN IPFQMLLRGA NGVAYSSLPD NAIDHFVKQA 660
KDNGVDIFRV FDALNDLEQL KVGVDAVKKA GGVVEATVCF SGDMLQPGKK YNLDYYLEIA 720
EKIVQMGTHI LGIKDMAGTM KPAAAKLLIG SLRAKYPDLP IHVHTHDSAG TAVASMTACA 780
LAGADVVDVA INSMSGLTSQ PSINALLASL EGNIDTGINV EHVRELDAYW AEMRLLYSCF 840
EADLKGPDPE VYQHEIPGGQ LTNLLFQAQQ LGLGEQWAET KRAYREANYL LGDIVKVTPT 900
SKVVGDLAQF MVSNKLTSDD VRRLANSLDF PDSVMDFFEG LIGQPYGGFP EPFRSDVLRN 960
KRRKLTCRPG LELEPFDLEK IREDLQNRFG DVDECDVASY NMYPRVYEDF QKMRETYGDL 1020
SVLPTRSFLS PLETDEEIEV VIEQGKTLII KLQAVGDLNK KTGEREVYFD LNGEMRKIRV 1080
ADRSQKVETV TKSKADMHDP LHIGAPMAGV IVEVKVHKGS LIKKGQPVAV LSAMKMEMII 1140
SSPSDGQVKE VFVSDGENVD SSDLLVLLED QVPVETKA 1178 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 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; IDA:SGD.
 GO:0006094; P:gluconeogenesis; IMP:SGD. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR011761; ATP-grasp.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR001882; Biotin_BS.
 IPR011764; Biotin_carboxylation_dom.
 IPR005482; Biotin_COase_C.
 IPR000089; Biotin_lipoyl.
 IPR005481; CarbamoylP_synth_lsu_N.
 IPR003379; Carboxylase_cons_dom.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR009057; Homeodomain-like.
 IPR016185; PreATP-grasp_dom.
 IPR000891; PYR_CT.
 IPR005930; Pyruv_COase.
 IPR011054; Rudment_hybrid_motif.
 IPR011053; Single_hybrid_motif. 
Pfam
 PF02785; Biotin_carb_C
 PF00364; Biotin_lipoyl
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2
 PF00682; HMGL-like
 PF02436; PYC_OADA 
SMART
 SM00878; Biotin_carb_C 
PROSITE
 PS50975; ATP_GRASP
 PS50979; BC
 PS00188; BIOTIN
 PS50968; BIOTINYL_LIPOYL
 PS50989; COA_CT_CTER
 PS50980; COA_CT_NTER
 PS00866; CPSASE_1
 PS00867; CPSASE_2
 PS50991; PYR_CT 
PRINTS