CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006162
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Urea amidolyase 
Protein Synonyms/Alias
 Urea carboxylase; Allophanate hydrolase 
Gene Name
 DUR1,2 
Gene Synonyms/Alias
 YBR208C; YBR1448 
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
69LHQFQILKSRENKETacetylation[1]
154KTPCAFSKEHVSGGSacetylation[1]
526LCTTKTSKAYQLFALacetylation[1]
880PAPNLPEKTRLALRKubiquitination[2]
1700VYKVNIEKSVFDHQEacetylation[1]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Hydrolysis of urea to ammonia and CO(2). 
Sequence Annotation
 DOMAIN 632 1075 Biotin carboxylation.
 DOMAIN 751 948 ATP-grasp.
 DOMAIN 1755 1835 Biotinyl-binding.
 NP_BIND 122 129 ATP (Potential).
 BINDING 747 747 ATP (By similarity).
 BINDING 830 830 ATP (By similarity).
 BINDING 865 865 ATP (By similarity).
 MOD_RES 803 803 Phosphoserine.
 MOD_RES 1798 1798 N6-biotinyllysine.  
Keyword
 Arginine metabolism; ATP-binding; Biotin; Complete proteome; Hydrolase; Ligase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1835 AA 
Protein Sequence
MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN AWISLISKEN 60
LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA CPSFAYEPSK DSKVVELLRN 120
AGAIIVGKTN LDQFATGLVG TRSPYGKTPC AFSKEHVSGG SSAGSASVVA RGIVPIALGT 180
DTAGSGRVPA ALNNLIGLKP TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP 240
DPDNDEYSRP YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI 300
DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK KYSAVDCFSF 360
EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV LVNSRQGTWT NFVNLADLAA 420
LAVPAGFRDD GLPNGITLIG KKFTDYALLE LANRYFQNIF PNGSRTYGTF TSSSVKPAND 480
QLVGPDYDPS TSIKLAVVGA HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL 540
KPGLRRVQDS NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG 600
YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK TLKKLGIRSV 660
AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA AKQTNAQAII PGYGFLSENA 720
DFSDACTSAG ITFVGPSGDI IRGLGLKHSA RQIAQKAGVP LVPGSLLITS VEEAKKVAAE 780
LEYPVMVKST AGGGGIGLQK VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE 840
VQLMGDGFGK AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC 900
AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND APDFDSTKVE 960
VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW VKKGTNISPE YDPTLAKIIV 1020
HGKDRDDAIS KLNQALEETK VYGCITNIDY LKSIITSDFF AKAKVSTNIL NSYQYEPTAI 1080
EITLPGAHTS IQDYPGRVGY WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS 1140
IVFHCETVIA ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV 1200
PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS LIPQISETKE 1260
WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV RLIGPKPKWA RSNGGEGGMH 1320
PSNTHDYVYS LGAINFTGDE PVIITCDGPS LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV 1380
PLSYESSRSL KESQDVAIKS LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ 1440
AGDRYVLVEY GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK 1500
ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS SAPWLPNNVD 1560
FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL DPRHRFLGSK YNPSRTYTER 1620
GAVGIGGMYM CIYAANSPGG YQLVGRTIPI WDKLCLAASS EVPWLMNPFD QVEFYPVSEE 1680
DLDKMTEDCD NGVYKVNIEK SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN 1740
ANSELKESVT VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE 1800
MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA 1835 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0004039; F:allophanate hydrolase activity; IMP:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
 GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0004847; F:urea carboxylase activity; IMP:SGD.
 GO:0000256; P:allantoin catabolic process; TAS:SGD.
 GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
 GO:0043419; P:urea catabolic process; IMP:SGD. 
Interpro
 IPR003833; Allophan_hydro_1.
 IPR003778; Allophan_hydro_2.
 IPR014085; Allophanate_hydrolase.
 IPR000120; Amidase.
 IPR023631; Amidase_dom.
 IPR024946; Arg_repress_C-like.
 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.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR016185; PreATP-grasp_dom.
 IPR011054; Rudment_hybrid_motif.
 IPR011053; Single_hybrid_motif.
 IPR014084; Urea_COase. 
Pfam
 PF02682; AHS1
 PF02626; AHS2
 PF01425; Amidase
 PF02785; Biotin_carb_C
 PF00364; Biotin_lipoyl
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2 
SMART
 SM00796; AHS1
 SM00797; AHS2
 SM00878; Biotin_carb_C 
PROSITE
 PS50975; ATP_GRASP
 PS50979; BC
 PS00188; BIOTIN
 PS50968; BIOTINYL_LIPOYL
 PS00866; CPSASE_1
 PS00867; CPSASE_2 
PRINTS