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P08680

- HEM0_MOUSE

UniProt

P08680 - HEM0_MOUSE

Protein

5-aminolevulinate synthase, erythroid-specific, mitochondrial

Gene

Alas2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei163 – 1631SubstrateBy similarity
    Binding sitei280 – 2801SubstrateBy similarity
    Binding sitei299 – 2991SubstrateBy similarity
    Binding sitei332 – 3321Pyridoxal phosphateBy similarity
    Binding sitei360 – 3601Pyridoxal phosphateBy similarity
    Binding sitei388 – 3881Pyridoxal phosphateBy similarity
    Active sitei391 – 3911By similarity
    Binding sitei420 – 4201Pyridoxal phosphateBy similarity
    Binding sitei421 – 4211Pyridoxal phosphateBy similarity
    Binding sitei508 – 5081SubstrateBy similarity

    GO - Molecular functioni

    1. 5-aminolevulinate synthase activity Source: UniProtKB
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. cellular iron ion homeostasis Source: MGI
    2. erythrocyte differentiation Source: UniProtKB
    3. heme biosynthetic process Source: UniProtKB
    4. hemoglobin biosynthetic process Source: UniProtKB
    5. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    6. response to hypoxia Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Heme biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_203298. Heme biosynthesis.
    UniPathwayiUPA00251; UER00375.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-aminolevulinate synthase, erythroid-specific, mitochondrial (EC:2.3.1.37)
    Short name:
    ALAS-E
    Alternative name(s):
    5-aminolevulinic acid synthase 2
    Delta-ALA synthase 2
    Delta-aminolevulinate synthase 2
    Gene namesi
    Name:Alas2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:87990. Alas2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi391 – 3911K → A or H: Abolishes enzyme activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4949Mitochondrion1 PublicationAdd
    BLAST
    Chaini50 – 5875385-aminolevulinate synthase, erythroid-specific, mitochondrialPRO_0000001224Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei391 – 3911N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP08680.
    PRIDEiP08680.

    PTM databases

    PhosphoSiteiP08680.

    Expressioni

    Tissue specificityi

    Erythroid specific.

    Gene expression databases

    ArrayExpressiP08680.
    BgeeiP08680.
    CleanExiMM_ALAS2.
    GenevestigatoriP08680.

    Interactioni

    Subunit structurei

    Interacts with SUCLA2 By similarity. Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi198059. 1 interaction.

    Structurei

    Secondary structure

    1
    587
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni5 – 84
    Beta strandi14 – 163
    Turni23 – 275
    Helixi28 – 325

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H7DNMR-A1-49[»]
    1H7JNMR-A1-26[»]
    ProteinModelPortaliP08680.
    SMRiP08680. Positions 1-49, 151-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08680.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0156.
    GeneTreeiENSGT00530000063111.
    HOGENOMiHOG000221020.
    HOVERGENiHBG005954.
    InParanoidiP08680.
    KOiK00643.
    OMAiHYLQSIN.
    OrthoDBiEOG7TQV0F.
    PhylomeDBiP08680.
    TreeFamiTF300724.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
    IPR015118. 5aminolev_synth_preseq.
    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.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    PF09029. Preseq_ALAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
    PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08680-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAAAMLLRS CPVLSQGPTG LLGKVAKTYQ FLFSIGRCPI LATQGPTCSQ    50
    IHLKATKAGG DSPSWAKSHC PFMLSELQDR KSKIVQRAAP EVQEDVKTFK 100
    TDLLSTMDST TRSHSFPSFQ EPEQTEGAVP HLIQNNMTGS QAFGYDQFFR 150
    DKIMEKKQDH TYRVFKTVNR WANAYPFAQH FSEASMASKD VSVWCSNDYL 200
    GISRHPRVLQ AIEETLKNHG AGAGGTRNIS GTSKFHVELE QELAELHQKD 250
    SALLFSSCFV ANDSTLFTLA KLLPGCEIYS DAGNHASMIQ GIRNSGAAKF 300
    VFRHNDPGHL KKLLEKSDPK TPKIVAFETV HSMDGAICPL EELCDVAHQY 350
    GALTFVDEVH AVGLYGARGA GIGERDGIMH KLDIISGTLG KAFGCVGGYI 400
    ASTRDLVDMV RSYAAGFIFT TSLPPMVLSG ALESVRLLKG EEGQALRRAH 450
    QRNVKHMRQL LMDRGFPVIP CPSHIIPIRV GNAALNSKIC DLLLSKHSIY 500
    VQAINYPTVP RGEELLRLAP SPHHSPQMME NFVEKLLLAW TEVGLPLQDV 550
    SVAACNFCHR PVHFELMSEW ERSYFGNMGP QYVTTYA 587
    Length:587
    Mass (Da):64,753
    Last modified:January 23, 2002 - v3
    Checksum:iA878D79FAD5B9856
    GO

    Sequence cautioni

    The sequence AAA37207.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 7515Missing in AAA37207. (PubMed:3557128)CuratedAdd
    BLAST
    Sequence conflicti66 – 661A → R in BAB22254. (PubMed:16141072)Curated
    Sequence conflicti171 – 1711W → R in AAA91866. 1 PublicationCurated
    Sequence conflicti338 – 3381C → V in AAA91866. 1 PublicationCurated
    Sequence conflicti368 – 3725RGAGI → GVQVS in AAA91866. 1 PublicationCurated
    Sequence conflicti427 – 4271V → M in AAA37207. (PubMed:3557128)Curated
    Sequence conflicti479 – 4791R → W in AAA91866. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15268 mRNA. Translation: AAA37207.1. Different initiation.
    M63244 mRNA. Translation: AAA91866.1.
    AK002642 mRNA. Translation: BAB22254.1.
    AK077610 mRNA. Translation: BAC36898.1.
    CCDSiCCDS41173.1.
    PIRiA29040. SYMSAL.
    RefSeqiNP_001095916.1. NM_001102446.1.
    NP_033783.1. NM_009653.3.
    UniGeneiMm.302724.

    Genome annotation databases

    EnsembliENSMUST00000066337; ENSMUSP00000066040; ENSMUSG00000025270.
    GeneIDi11656.
    KEGGimmu:11656.
    UCSCiuc009uoj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15268 mRNA. Translation: AAA37207.1 . Different initiation.
    M63244 mRNA. Translation: AAA91866.1 .
    AK002642 mRNA. Translation: BAB22254.1 .
    AK077610 mRNA. Translation: BAC36898.1 .
    CCDSi CCDS41173.1.
    PIRi A29040. SYMSAL.
    RefSeqi NP_001095916.1. NM_001102446.1.
    NP_033783.1. NM_009653.3.
    UniGenei Mm.302724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H7D NMR - A 1-49 [» ]
    1H7J NMR - A 1-26 [» ]
    ProteinModelPortali P08680.
    SMRi P08680. Positions 1-49, 151-540.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198059. 1 interaction.

    PTM databases

    PhosphoSitei P08680.

    Proteomic databases

    PaxDbi P08680.
    PRIDEi P08680.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000066337 ; ENSMUSP00000066040 ; ENSMUSG00000025270 .
    GeneIDi 11656.
    KEGGi mmu:11656.
    UCSCi uc009uoj.1. mouse.

    Organism-specific databases

    CTDi 212.
    MGIi MGI:87990. Alas2.

    Phylogenomic databases

    eggNOGi COG0156.
    GeneTreei ENSGT00530000063111.
    HOGENOMi HOG000221020.
    HOVERGENi HBG005954.
    InParanoidi P08680.
    KOi K00643.
    OMAi HYLQSIN.
    OrthoDBi EOG7TQV0F.
    PhylomeDBi P08680.
    TreeFami TF300724.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00375 .
    Reactomei REACT_203298. Heme biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P08680.
    NextBioi 279269.
    PROi P08680.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08680.
    Bgeei P08680.
    CleanExi MM_ALAS2.
    Genevestigatori P08680.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR010961. 4pyrrol_synth_NH2levulA_synth.
    IPR015118. 5aminolev_synth_preseq.
    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.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    PF09029. Preseq_ALAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01821. 5aminolev_synth. 1 hit.
    PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of mouse 5-aminolevulinic acid synthase cDNA and expression of its gene in hepatic and erythroid tissues."
      Schoenhaut D.S., Curtis P.J.
      Gene 48:55-63(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Two genes encode Ala synthase in DBA/2 mouse: housekeeping and erythroid-specific."
      Young E.G., Dierks P.M.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: DBA/2.
      Tissue: Erythroleukemia.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Kidney.
    4. "Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase."
      Ferreira G.C., Neame P.J., Dailey H.A.
      Protein Sci. 2:1959-1965(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PYRIDOXAL PHOSPHATE AT LYS-391.
    5. "The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase."
      Goodfellow B.J., Dias J.S., Ferreira G.C., Henklein P., Wray V., Macedo A.L.
      FEBS Lett. 505:325-331(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-49, TRANSIT PEPTIDE CLEAVAGE SITE.

    Entry informationi

    Entry nameiHEM0_MOUSE
    AccessioniPrimary (citable) accession number: P08680
    Secondary accession number(s): Q64452, Q9DCN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3