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Protein

5-aminolevulinate synthase, mitochondrial

Gene

HEM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.1 Publication

Miscellaneous

Present with 22600 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Ihnhibited by hemin.1 Publication

Kineticsi

  1. KM=3 mM for glycine1 Publication
  2. KM=2 µM for succinyl-CoA1 Publication

    pH dependencei

    Optimum pH is 7.4.1 Publication

    Pathwayi: protoporphyrin-IX biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from glycine.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. 5-aminolevulinate synthase, mitochondrial (HEM1)
    This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from glycine, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei91SubstrateBy similarity1
    Binding sitei204SubstrateBy similarity1
    Binding sitei223SubstrateBy similarity1
    Binding sitei256Pyridoxal phosphateBy similarity1
    Binding sitei284Pyridoxal phosphateBy similarity1
    Binding sitei334Pyridoxal phosphateBy similarity1
    Active sitei337By similarity1
    Binding sitei366Pyridoxal phosphate; shared with dimeric partnerBy similarity1
    Binding sitei367Pyridoxal phosphate; shared with dimeric partnerBy similarity1
    Binding sitei452SubstrateBy similarity1

    GO - Molecular functioni

    • 5-aminolevulinate synthase activity Source: SGD
    • pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    • heme biosynthetic process Source: SGD
    • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processHeme biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyciYEAST:YDR232W-MONOMER
    ReactomeiR-SCE-189451 Heme biosynthesis
    UniPathwayiUPA00251; UER00375

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-aminolevulinate synthase, mitochondrial1 Publication (EC:2.3.1.371 Publication)
    Alternative name(s):
    5-aminolevulinic acid synthase
    Delta-ALA synthase
    Delta-aminolevulinate synthase
    Gene namesi
    Name:HEM11 Publication
    Synonyms:CYD1
    Ordered Locus Names:YDR232WImported
    ORF Names:YD9934.16
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDR232W
    SGDiS000002640 HEM1

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    In combination with a disruption of MCX1, abrogates mitochondrial respiration.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi275G → R: Lethal in combination with a MCX1 disruption. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 22MitochondrionSequence analysisAdd BLAST22
    ChainiPRO_000000124523 – 5485-aminolevulinate synthase, mitochondrialAdd BLAST526

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei337N6-(pyridoxal phosphate)lysineBy similarity1

    Proteomic databases

    MaxQBiP09950
    PaxDbiP09950
    PRIDEiP09950

    Interactioni

    Subunit structurei

    Homodimer (PubMed:6381051). Interacts with MCX1 (PubMed:25957689).2 Publications

    Protein-protein interaction databases

    BioGridi32283, 191 interactors
    IntActiP09950, 6 interactors
    STRINGi4932.YDR232W

    Structurei

    Secondary structure

    1548
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi73 – 86Combined sources14
    Beta strandi100 – 102Combined sources3
    Beta strandi105 – 107Combined sources3
    Beta strandi114 – 117Combined sources4
    Helixi126 – 128Combined sources3
    Helixi130 – 143Combined sources14
    Turni151 – 153Combined sources3
    Helixi158 – 171Combined sources14
    Beta strandi174 – 180Combined sources7
    Helixi182 – 196Combined sources15
    Beta strandi201 – 205Combined sources5
    Helixi210 – 219Combined sources10
    Beta strandi221 – 226Combined sources6
    Helixi231 – 239Combined sources9
    Beta strandi247 – 255Combined sources9
    Turni256 – 259Combined sources4
    Helixi264 – 274Combined sources11
    Beta strandi276 – 281Combined sources6
    Turni283 – 288Combined sources6
    Helixi296 – 300Combined sources5
    Helixi302 – 308Combined sources7
    Helixi324 – 327Combined sources4
    Beta strandi329 – 337Combined sources9
    Beta strandi344 – 348Combined sources5
    Helixi350 – 359Combined sources10
    Helixi361 – 364Combined sources4
    Helixi371 – 385Combined sources15
    Helixi389 – 408Combined sources20
    Beta strandi416 – 418Combined sources3
    Beta strandi420 – 423Combined sources4
    Helixi427 – 441Combined sources15
    Turni450 – 452Combined sources3
    Beta strandi459 – 462Combined sources4
    Helixi470 – 487Combined sources18
    Helixi492 – 497Combined sources6
    Helixi518 – 521Combined sources4
    Helixi525 – 527Combined sources3
    Helixi530 – 532Combined sources3
    Helixi541 – 543Combined sources3

    3D structure databases

    ProteinModelPortaliP09950
    SMRiP09950
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi26 – 62Ala-richPROSITE-ProRule annotationAdd BLAST37

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    GeneTreeiENSGT00530000063111
    HOGENOMiHOG000221020
    InParanoidiP09950
    KOiK00643
    OMAiKQDHTYR
    OrthoDBiEOG092C1OK6

    Family and domain databases

    Gene3Di3.40.640.10, 2 hits
    3.90.1150.10, 2 hits
    InterProiView protein in InterPro
    IPR010961 4pyrrol_synth_NH2levulA_synth
    IPR001917 Aminotrans_II_pyridoxalP_BS
    IPR004839 Aminotransferase_I/II
    IPR015424 PyrdxlP-dep_Trfase
    IPR015422 PyrdxlP-dep_Trfase_dom1
    IPR015421 PyrdxlP-dep_Trfase_major
    PfamiView protein in Pfam
    PF00155 Aminotran_1_2, 1 hit
    SUPFAMiSSF53383 SSF53383, 1 hit
    TIGRFAMsiTIGR01821 5aminolev_synth, 1 hit
    PROSITEiView protein in PROSITE
    PS00599 AA_TRANSFER_CLASS_2, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09950-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQRSIFARFG NSSAAVSTLN RLSTTAAPHA KNGYATATGA GAAAATATAS
    60 70 80 90 100
    STHAAAAAAA AANHSTQESG FDYEGLIDSE LQKKRLDKSY RYFNNINRLA
    110 120 130 140 150
    KEFPLAHRQR EADKVTVWCS NDYLALSKHP EVLDAMHKTI DKYGCGAGGT
    160 170 180 190 200
    RNIAGHNIPT LNLEAELATL HKKEGALVFS SCYVANDAVL SLLGQKMKDL
    210 220 230 240 250
    VIFSDELNHA SMIVGIKHAN VKKHIFKHND LNELEQLLQS YPKSVPKLIA
    260 270 280 290 300
    FESVYSMAGS VADIEKICDL ADKYGALTFL DEVHAVGLYG PHGAGVAEHC
    310 320 330 340 350
    DFESHRASGI ATPKTNDKGG AKTVMDRVDM ITGTLGKSFG SVGGYVAASR
    360 370 380 390 400
    KLIDWFRSFA PGFIFTTTLP PSVMAGATAA IRYQRCHIDL RTSQQKHTMY
    410 420 430 440 450
    VKKAFHELGI PVIPNPSHIV PVLIGNADLA KQASDILINK HQIYVQAINF
    460 470 480 490 500
    PTVARGTERL RITPTPGHTN DLSDILINAV DDVFNELQLP RVRDWESQGG
    510 520 530 540
    LLGVGESGFV EESNLWTSSQ LSLTNDDLNP NVRDPIVKQL EVSSGIKQ
    Length:548
    Mass (Da):59,362
    Last modified:July 1, 1989 - v1
    Checksum:iFAAEDBAFCEDBE429
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti181S → P in AAU09697 (PubMed:17322287).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26329 Genomic DNA Translation: AAA34668.1
    Z48612 Genomic DNA Translation: CAA88511.1
    AY723780 Genomic DNA Translation: AAU09697.1
    J03556 Genomic DNA No translation available.
    BK006938 Genomic DNA Translation: DAA12073.1
    PIRiA24870 SYBYAL
    RefSeqiNP_010518.1, NM_001180540.1

    Genome annotation databases

    EnsemblFungiiYDR232W; YDR232W; YDR232W
    GeneIDi851818
    KEGGisce:YDR232W

    Similar proteinsi

    Entry informationi

    Entry nameiHEM1_YEAST
    AccessioniPrimary (citable) accession number: P09950
    Secondary accession number(s): D6VSL3, E9P946
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: July 18, 2018
    This is version 169 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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