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P30949

- GSA_BACSU

UniProt

P30949 - GSA_BACSU

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

    Cofactori

    Pyridoxal phosphate.By similarity

    Pathwayi

    GO - Molecular functioni

    1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: InterPro
    3. transaminase activity Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciBSUB:BSU28120-MONOMER.
    UniPathwayiUPA00251; UER00317.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
    Short name:
    GSA
    Alternative name(s):
    Glutamate-1-semialdehyde aminotransferase
    Short name:
    GSA-AT
    Gene namesi
    Name:hemL
    Synonyms:hemK
    Ordered Locus Names:BSU28120
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU28120. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120393Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP30949.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi224308.BSU28120.

    Structurei

    Secondary structure

    1
    430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1511
    Helixi19 – 213
    Beta strandi22 – 243
    Helixi25 – 284
    Turni30 – 334
    Beta strandi39 – 446
    Beta strandi46 – 494
    Beta strandi54 – 596
    Helixi60 – 623
    Helixi72 – 8413
    Helixi93 – 10513
    Beta strandi110 – 1167
    Helixi118 – 13316
    Beta strandi137 – 1426
    Helixi150 – 1523
    Beta strandi158 – 1614
    Beta strandi165 – 1684
    Beta strandi179 – 1835
    Helixi187 – 19711
    Helixi198 – 2003
    Beta strandi201 – 2066
    Beta strandi208 – 2103
    Beta strandi212 – 2143
    Helixi222 – 23312
    Beta strandi236 – 2405
    Turni242 – 2476
    Helixi252 – 2565
    Beta strandi262 – 2665
    Helixi268 – 2714
    Beta strandi277 – 2815
    Helixi283 – 2864
    Turni290 – 2923
    Beta strandi293 – 2953
    Helixi305 – 31612
    Helixi320 – 34324
    Beta strandi349 – 3535
    Beta strandi356 – 3649
    Helixi369 – 3724
    Helixi377 – 38913
    Beta strandi396 – 4005
    Helixi410 – 42920

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BS8X-ray2.30A1-430[»]
    ProteinModelPortaliP30949.
    SMRiP30949. Positions 1-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30949.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0001.
    HOGENOMiHOG000020210.
    KOiK01845.
    OMAiRAIKPYP.
    OrthoDBiEOG6QVRHN.
    PhylomeDBiP30949.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPiMF_00375. HemL_aminotrans_3.
    InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00713. hemL. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30949-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSYEKSKTA FKEAQKLMPG GVNSPVRAFK SVDMDPIFME RGKGSKIFDI    50
    DGNEYIDYVL SWGPLILGHT NDRVVESLKK VAEYGTSFGA PTEVENELAK 100
    LVIDRVPSVE IVRMVSSGTE ATMSALRLAR GYTGRNKILK FEGCYHGHGD 150
    SLLIKAGSGV ATLGLPDSPG VPEGIAKNTI TVPYNDLESV KLAFQQFGED 200
    IAGVIVEPVA GNMGVVPPQE GFLQGLRDIT EQYGSLLIFD EVMTGFRVDY 250
    NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKAEIMEQIA PSGPIYQAGT 300
    LSGNPLAMTA GLETLKQLTP ESYKNFIKKG DRLEEGISKT AGAHGIPHTF 350
    NRAGSMIGFF FTNEPVINYE TAKSSDLKLF ASYYKGMANE GVFLPPSQFE 400
    GLFLSTAHTD EDIENTIQAA EKVFAEISRR 430
    Length:430
    Mass (Da):46,449
    Last modified:July 1, 1993 - v1
    Checksum:iFBC7CF1784C46017
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57676 Genomic DNA. Translation: AAA22515.1.
    AL009126 Genomic DNA. Translation: CAB14772.1.
    PIRiD42728.
    RefSeqiNP_390690.1. NC_000964.3.
    WP_004398699.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14772; CAB14772; BSU28120.
    GeneIDi937490.
    KEGGibsu:BSU28120.
    PATRICi18977500. VBIBacSub10457_2939.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57676 Genomic DNA. Translation: AAA22515.1 .
    AL009126 Genomic DNA. Translation: CAB14772.1 .
    PIRi D42728.
    RefSeqi NP_390690.1. NC_000964.3.
    WP_004398699.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BS8 X-ray 2.30 A 1-430 [» ]
    ProteinModelPortali P30949.
    SMRi P30949. Positions 1-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU28120.

    Proteomic databases

    PaxDbi P30949.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14772 ; CAB14772 ; BSU28120 .
    GeneIDi 937490.
    KEGGi bsu:BSU28120.
    PATRICi 18977500. VBIBacSub10457_2939.

    Organism-specific databases

    GenoListi BSU28120. [Micado ]

    Phylogenomic databases

    eggNOGi COG0001.
    HOGENOMi HOG000020210.
    KOi K01845.
    OMAi RAIKPYP.
    OrthoDBi EOG6QVRHN.
    PhylomeDBi P30949.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci BSUB:BSU28120-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P30949.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPi MF_00375. HemL_aminotrans_3.
    InterProi IPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00713. hemL. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III."
      Hansson M., Rutberg L., Schroeder I., Hederstedt L.
      J. Bacteriol. 173:2590-2599(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.

    Entry informationi

    Entry nameiGSA_BACSU
    AccessioniPrimary (citable) accession number: P30949
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    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