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Q06965

- HEM0_RHOS4

UniProt

Q06965 - HEM0_RHOS4

Protein

5-aminolevulinate synthase 2

Gene

hemT

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 sitei21 – 211SubstrateBy similarity
    Binding sitei137 – 1371SubstrateBy similarity
    Binding sitei189 – 1891Pyridoxal phosphateBy similarity
    Binding sitei217 – 2171Pyridoxal phosphateBy similarity
    Binding sitei245 – 2451Pyridoxal phosphateBy similarity
    Active sitei248 – 2481By similarity
    Binding sitei277 – 2771Pyridoxal phosphateBy similarity
    Binding sitei278 – 2781Pyridoxal phosphateBy similarity
    Binding sitei363 – 3631SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Heme biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13234.
    RSPH272943:GJAS-3162-MONOMER.
    UniPathwayiUPA00251; UER00375.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-aminolevulinate synthase 2 (EC:2.3.1.37)
    Alternative name(s):
    5-aminolevulinic acid synthase
    Delta-ALA synthase
    Delta-aminolevulinate synthase
    Gene namesi
    Name:hemT
    Ordered Locus Names:RHOS4_30750
    ORF Names:RSP_3028
    OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
    Taxonomic identifieri272943 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
    ProteomesiUP000002703: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4074075-aminolevulinate synthase 2PRO_0000163830Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Protein-protein interaction databases

    STRINGi272943.RSP_3028.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06965.
    SMRiQ06965. Positions 2-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0156.
    HOGENOMiHOG000221020.
    KOiK00643.
    OMAiLCRSISE.
    OrthoDBiEOG6Q8HZD.
    PhylomeDBiQ06965.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR010961. 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.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 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.

    Q06965-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEFSQHFQKL IDDMRLDGRY RTFAELERIA GEFPTALWHG PDGQARRVTV    50
    WCSNDYLGMG QNAEVLAAMH RSIDLSGAGT GGTRNISGTN RQHVALEAEL 100
    ADLHGKESAL IFTSGWISNL AALGTLGKIL PECAIFSDAL NHNSMIEGIR 150
    RSGAERFIFH HNDPVHLDRL LSSVDPARPK IVAFESVYSM DGDIAPIAEI 200
    CDVAERHGAL TYLDEVHAVG LYGPRGGGIS DRDGLADRVT IIEGTLAKAF 250
    GVMGGYVSGP SLLMDVIRSM SDSFIFTTSI CPHLAAGALA AVRHVKAHPD 300
    ERRRQAENAV RLKVLLQKAG LPVLDTPSHI LPVMVGEAHL CRSISEALLA 350
    RHAIYVQPIN YPTVARGQER FRLTPTPFHT TSHMEALVEA LLAVGRDLGW 400
    AMSRRAA 407
    Length:407
    Mass (Da):44,333
    Last modified:October 1, 1996 - v1
    Checksum:i4772E3EC1DA55D82
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07489 Genomic DNA. Translation: AAA26124.1.
    CP000144 Genomic DNA. Translation: ABA80643.1.
    PIRiA49845.
    RefSeqiWP_011338981.1. NZ_AKVW01000002.1.
    YP_354544.1. NC_007494.2.

    Genome annotation databases

    EnsemblBacteriaiABA80643; ABA80643; RSP_3028.
    GeneIDi3721613.
    KEGGirsp:RSP_3028.
    PATRICi23156193. VBIRhoSph57909_3445.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07489 Genomic DNA. Translation: AAA26124.1 .
    CP000144 Genomic DNA. Translation: ABA80643.1 .
    PIRi A49845.
    RefSeqi WP_011338981.1. NZ_AKVW01000002.1.
    YP_354544.1. NC_007494.2.

    3D structure databases

    ProteinModelPortali Q06965.
    SMRi Q06965. Positions 2-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272943.RSP_3028.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA80643 ; ABA80643 ; RSP_3028 .
    GeneIDi 3721613.
    KEGGi rsp:RSP_3028.
    PATRICi 23156193. VBIRhoSph57909_3445.

    Phylogenomic databases

    eggNOGi COG0156.
    HOGENOMi HOG000221020.
    KOi K00643.
    OMAi LCRSISE.
    OrthoDBi EOG6Q8HZD.
    PhylomeDBi Q06965.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00375 .
    BioCyci MetaCyc:MONOMER-13234.
    RSPH272943:GJAS-3162-MONOMER.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi 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.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 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. "Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes."
      Neidle E.L., Kaplan S.
      J. Bacteriol. 175:2292-2303(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

    Entry informationi

    Entry nameiHEM0_RHOS4
    AccessioniPrimary (citable) accession number: Q06965
    Secondary accession number(s): Q3IXU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Expressed in the mutant strain HemA1 but expression in the wild-type strain has not been proven.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3