CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001813
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histidine biosynthesis trifunctional protein 
Protein Synonyms/Alias
 Phosphoribosyl-AMP cyclohydrolase; Phosphoribosyl-ATP pyrophosphohydrolase; Histidinol dehydrogenase; HDH 
Gene Name
 HIS4 
Gene Synonyms/Alias
 YCL030C; YCL183; YCL30C 
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
137LSKDMLTKEVLGEVRacetylation[1]
176SSKKSIAKAIDLGRGacetylation[1]
278DSALLDAKIKEEAEEacetylation[1]
280ALLDAKIKEEAEELTacetylation[1]
318VANDVSLKDVENNLNacetylation[1]
327VENNLNMKHLKVTRRacetylation[1]
352QPKAEEEKLTGPIHLacetylation[1]
372SDKVGVQKALSRPIQubiquitination[2]
409ALLEYTEKFDGVKLSacetylation[1]
563ETIPKVDKILGPGNQubiquitination[2]
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
  
Sequence Annotation
 REGION 1 229 Phosphoribosyl-AMP cyclohydrolase.
 REGION 230 312 Phosphoribosyl-ATP pyrophosphohydrolase.
 REGION 313 799 Histidinol dehydrogenase.
 ACT_SITE 687 687 By similarity.
 ACT_SITE 688 688 By similarity.
 METAL 618 618 Zinc (By similarity).
 METAL 621 621 Zinc (By similarity).
 METAL 721 721 Zinc (By similarity).
 METAL 780 780 Zinc (By similarity).  
Keyword
 Amino-acid biosynthesis; ATP-binding; Complete proteome; Histidine biosynthesis; Hydrolase; Metal-binding; Multifunctional enzyme; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 799 AA 
Protein Sequence
MVLPILPLID DLASWNSKKE YVSLVGQVLL DGSSLSNEEI LQFSKEEEVP LVALSLPSGK 60
FSDDEIIAFL NNGVSSLFIA SQDAKTAEHL VEQLNVPKER VVVEENGVFS NQFMVKQKFS 120
QDKIVSIKKL SKDMLTKEVL GEVRTDRPDG LYTTLVVDQY ERCLGLVYSS KKSIAKAIDL 180
GRGVYYSRSR NEIWIKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE 240
FKHGLVGLES LLKQRLQDAP EESYTRRLFN DSALLDAKIK EEAEELTEAK GKKELSWEAA 300
DLFYFALAKL VANDVSLKDV ENNLNMKHLK VTRRKGDAKP KFVGQPKAEE EKLTGPIHLD 360
VVKASDKVGV QKALSRPIQK TSEIMHLVNP IIENVRDKGN SALLEYTEKF DGVKLSNPVL 420
NAPFPEEYFE GLTEEMKEAL DLSIENVRKF HAAQLPTETL EVETQPGVLC SRFPRPIEKV 480
GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGASKIV 540
LAGGAQAVAA MAYGTETIPK VDKILGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 600
IADEDADVDF VASDLLSQAE HGIDSQVILV GVNLSEKKIQ EIQDAVHNQA LQLPRVDIVR 660
KCIAHSTIVL CDGYEEALEM SNQYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG 720
DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH 780
RNAVKIRMSK LGLIPKDFQ 799 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004399; F:histidinol dehydrogenase activity; IDA:SGD.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IDA:SGD.
 GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IDA:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0000105; P:histidine biosynthetic process; IMP:SGD. 
Interpro
 IPR016161; Ald_DH/histidinol_DH.
 IPR016298; Histidine_synth_trifunct.
 IPR001692; Histidinol_DH_CS.
 IPR012131; Hstdl_DH.
 IPR008179; PRib-ATP_PPHydrolase.
 IPR021130; PRib-ATP_PPHydrolase-like.
 IPR002496; PRib_AMP_CycHydrolase_dom. 
Pfam
 PF00815; Histidinol_dh
 PF01502; PRA-CH
 PF01503; PRA-PH 
SMART
  
PROSITE
 PS00611; HISOL_DEHYDROGENASE 
PRINTS
 PR00083; HOLDHDRGNASE.