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Q59292

- HEMA_CLOJO

UniProt

Q59292 - HEMA_CLOJO

Protein

Probable multifunctional siroheme biosynthesis protein HemA

Gene

hemA

Organism
Clostridium josui
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Multifunctional enzyme that catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA), the NAD-dependent ring dehydrogenation of precorrin-2 to sirohydrochlorin and finally, the ferrochelation of sirohydrochlorin to yield siroheme.1 Publication

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation
    Precorrin-2 + NAD+ = sirohydrochlorin + NADH.
    Siroheme + 2 H+ = sirohydrochlorin + Fe2+.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691NucleophileUniRule annotation
    Sitei117 – 1171Important for activityUniRule annotation
    Binding sitei127 – 1271Glutamyl-tRNABy similarity
    Binding sitei132 – 1321Glutamyl-tRNABy similarity
    Binding sitei138 – 1381Glutamyl-tRNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 272NADBy similarity
    Nucleotide bindingi47 – 482NADBy similarity
    Nucleotide bindingi206 – 2116NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro
    3. precorrin-2 dehydrogenase activity Source: UniProtKB-EC
    4. sirohydrochlorin ferrochelatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cobalamin biosynthetic process Source: UniProtKB-UniPathway
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    3. siroheme biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase, Oxidoreductase

    Keywords - Biological processi

    Cobalamin biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    UniPathwayiUPA00148; UER00222.
    UPA00251; UER00316.
    UPA00262; UER00222.
    UPA00262; UER00376.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable multifunctional siroheme biosynthesis protein HemA
    Including the following 3 domains:
    Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTRUniRule annotation
    Precorrin-2 dehydrogenase (EC:1.3.1.76)
    Sirohydrochlorin ferrochelatase (EC:4.99.1.4)
    Gene namesi
    Name:hemAUniRule annotation
    OrganismiClostridium josui
    Taxonomic identifieri1499 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 515515Probable multifunctional siroheme biosynthesis protein HemAPRO_0000114012Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ59292.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 174149Glutamyl-tRNA reductaseAdd
    BLAST
    Regioni68 – 714Glutamyl-tRNA bindingBy similarity
    Regioni367 – 507141Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseAdd
    BLAST

    Domaini

    Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamyl-tRNA reductase family.Curated
    In the C-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.Curated

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    IPR006367. Sirohaem_synthase_N.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    PF13241. NAD_binding_7. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01470. cysG_Nterm. 1 hit.
    TIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q59292-1 [UniParc]FASTAAdd to Basket

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    MQLGRHNSGS IKKRLEMYIL SIISASLDYK SAAIDIRERF SYTSTRIREI    50
    LRRIKAADGV SGAVLLCTCN RTELYISGDN IENMNPALLL CQLSGEEDHK 100
    SLMTLFSIRH DSEAIFHLME VACGLQSMVL FEDRVITQVK NAAAISREEK 150
    TIDSTLETLF RLCITAAKKA KTEIKVKAVP TSAAERAITE LSKKYCFTDK 200
    RILVIGNGEI GRLCCKKLIE LGAEITITLR KYKHGEIIIP VGCNTIPYDE 250
    REEVLPLSDV VISATTSPHF TITYDMIEKL ERKPEIFVDL ALPRDIESSI 300
    SNFTGVELYN LDRFYTDYSV LNQKEVSKIR EIINHFILQF EKWKDYREEA 350
    AFTKIPDLHN DTLYGRFPLF IDLSGKKVLV VGGGEIATRR VKTLLRFGAD 400
    IYLVAPHLTS ELQEMLNCKL INYREGYYES QDIQNMFLVI AATNDRETNH 450
    KVYLDAKEKG IQMSIADCRE ECSFYFPAIF EFDGIVGGLV SQNGDNHSLV 500
    KSVAEQIRKI GQATD 515
    Length:515
    Mass (Da):58,368
    Last modified:November 1, 1997 - v1
    Checksum:iA9769824AA30DC4C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28503 Genomic DNA. Translation: BAA05860.1.
    PIRiI40809.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28503 Genomic DNA. Translation: BAA05860.1 .
    PIRi I40809.

    3D structure databases

    ProteinModelPortali Q59292.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00222 .
    UPA00251 ; UER00316 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    IPR006367. Sirohaem_synthase_N.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    PF13241. NAD_binding_7. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01470. cysG_Nterm. 1 hit.
    TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
      Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.
      J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: FERM P-9684.

    Entry informationi

    Entry nameiHEMA_CLOJO
    AccessioniPrimary (citable) accession number: Q59292
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3