CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002842
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5-aminolevulinate synthase, mitochondrial 
Protein Synonyms/Alias
 5-aminolevulinic acid synthase; Delta-ALA synthase; Delta-aminolevulinate synthase 
Gene Name
 HEM1 
Gene Synonyms/Alias
 CYD1; YDR232W; YD9934.16 
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
142AMHKTIDKYGCGAGGacetylation[1]
337MITGTLGKSFGSVGGacetylation[1]
351GYVAASRKLIDWFRSacetylation[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
Functional Description
  
Sequence Annotation
 ACT_SITE 337 337 By similarity.
 BINDING 91 91 Substrate (By similarity).
 BINDING 204 204 Substrate (By similarity).
 BINDING 223 223 Substrate (By similarity).
 BINDING 256 256 Pyridoxal phosphate (By similarity).
 BINDING 284 284 Pyridoxal phosphate (By similarity).
 BINDING 334 334 Pyridoxal phosphate (By similarity).
 BINDING 366 366 Pyridoxal phosphate (By similarity).
 BINDING 367 367 Pyridoxal phosphate (By similarity).
 BINDING 452 452 Substrate (By similarity).
 MOD_RES 337 337 N6-(pyridoxal phosphate)lysine  
Keyword
 Acyltransferase; Complete proteome; Heme biosynthesis; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 548 AA 
Protein Sequence
MQRSIFARFG NSSAAVSTLN RLSTTAAPHA KNGYATATGA GAAAATATAS STHAAAAAAA 60
AANHSTQESG FDYEGLIDSE LQKKRLDKSY RYFNNINRLA KEFPLAHRQR EADKVTVWCS 120
NDYLALSKHP EVLDAMHKTI DKYGCGAGGT RNIAGHNIPT LNLEAELATL HKKEGALVFS 180
SCYVANDAVL SLLGQKMKDL VIFSDELNHA SMIVGIKHAN VKKHIFKHND LNELEQLLQS 240
YPKSVPKLIA FESVYSMAGS VADIEKICDL ADKYGALTFL DEVHAVGLYG PHGAGVAEHC 300
DFESHRASGI ATPKTNDKGG AKTVMDRVDM ITGTLGKSFG SVGGYVAASR KLIDWFRSFA 360
PGFIFTTTLP PSVMAGATAA IRYQRCHIDL RTSQQKHTMY VKKAFHELGI PVIPNPSHIV 420
PVLIGNADLA KQASDILINK HQIYVQAINF PTVARGTERL RITPTPGHTN DLSDILINAV 480
DDVFNELQLP RVRDWESQGG LLGVGESGFV EESNLWTSSQ LSLTNDDLNP NVRDPIVKQL 540
EVSSGIKQ 548 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:SGD.
 GO:0003870; F:5-aminolevulinate synthase activity; IDA:SGD.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006783; P:heme biosynthetic process; IMP:SGD.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR010961; 4pyrrol_synth_NH2levulA_synth.
 IPR001917; Aminotrans_II_pyridoxalP_BS.
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00599; AA_TRANSFER_CLASS_2 
PRINTS