Tag | Content |
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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 |
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142 | AMHKTIDKYGCGAGG | acetylation | [1] | 337 | MITGTLGKSFGSVGG | acetylation | [1] | 351 | GYVAASRKLIDWFRS | acetylation | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |