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P24630

- GSA_SYNP6

UniProt

P24630 - GSA_SYNP6

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.

    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. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciSELO269084:GCDQ-897-MONOMER.
    UniPathwayiUPA00251; UER00317.
    UPA00668.

    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:gsa
    Ordered Locus Names:syc0881_c
    OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
    Taxonomic identifieri269084 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000001175: Chromosome

    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
    Initiator methioninei1 – 11Removed
    Chaini2 – 433432Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120461Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei273 – 2731N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi269084.syc0881_c.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 1910
    Turni20 – 223
    Helixi24 – 263
    Beta strandi27 – 293
    Helixi30 – 334
    Turni35 – 384
    Beta strandi44 – 496
    Beta strandi51 – 544
    Beta strandi59 – 646
    Helixi65 – 673
    Turni68 – 725
    Helixi77 – 8711
    Helixi98 – 11013
    Beta strandi115 – 1228
    Helixi123 – 13816
    Beta strandi142 – 1476
    Helixi155 – 1573
    Helixi164 – 1685
    Beta strandi174 – 1763
    Helixi178 – 1814
    Beta strandi184 – 1885
    Helixi192 – 20110
    Turni203 – 2053
    Beta strandi206 – 2116
    Beta strandi213 – 2153
    Beta strandi217 – 2193
    Helixi227 – 23711
    Beta strandi241 – 2455
    Turni247 – 2526
    Helixi257 – 2615
    Beta strandi267 – 2715
    Helixi273 – 2764
    Beta strandi277 – 2804
    Beta strandi282 – 2865
    Helixi288 – 2914
    Turni295 – 2973
    Beta strandi298 – 3003
    Turni305 – 3084
    Helixi310 – 32314
    Helixi328 – 34922
    Beta strandi355 – 3595
    Beta strandi362 – 3698
    Helixi375 – 3784
    Helixi383 – 39513
    Helixi416 – 43217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GSAX-ray2.40A/B2-433[»]
    3FQ7X-ray2.15A/B7-433[»]
    3FQ8X-ray2.00A/B7-433[»]
    3FQAX-ray2.35A/B7-433[»]
    3GSBX-ray3.00A/B2-433[»]
    4GSAX-ray2.50A/B2-433[»]
    ProteinModelPortaliP24630.
    SMRiP24630. Positions 7-433.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24630.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0001.
    HOGENOMiHOG000020210.
    KOiK01845.
    OrthoDBiEOG6QVRHN.

    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.

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

    P24630-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA    50
    YAWDVDGNRY IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE 100
    NVLAEMVIDA VPSIEMVRFV NSGTEACMAV LRLMRAYTGR DKIIKFEGCY 150
    HGHADMFLVK AGSGVATLGL PDSPGVPKST TANTLTAPYN DLEAVKALFA 200
    ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA LLVFDEVMTG 250
    FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM 300
    YQAGTLSGNP LAMTAGIKTL ELLRQPATYE YLDQITKRLS DGLLAIAQET 350
    GHAACGGQVS GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL 400
    APSQFEAGFT SLAHTEEDID ATLAAARTVM SAL 433
    Length:433
    Mass (Da):46,116
    Last modified:January 23, 2007 - v4
    Checksum:i83585133A666B923
    GO

    Sequence cautioni

    The sequence BAD79071.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511Y → I(PubMed:1900346)Curated
    Sequence conflicti51 – 511Y → I(PubMed:1905724)Curated
    Sequence conflicti108 – 1081I → N(PubMed:1900346)Curated
    Sequence conflicti108 – 1081I → N(PubMed:1905724)Curated
    Sequence conflicti133 – 1342LM → VV(PubMed:1900346)Curated
    Sequence conflicti133 – 1342LM → VV(PubMed:1905724)Curated
    Sequence conflicti172 – 1721D → S(PubMed:1900346)Curated
    Sequence conflicti172 – 1721D → S(PubMed:1905724)Curated
    Sequence conflicti179 – 1791S → K(PubMed:1900346)Curated
    Sequence conflicti179 – 1791S → K(PubMed:1905724)Curated
    Sequence conflicti187 – 1871A → T(PubMed:1900346)Curated
    Sequence conflicti187 – 1871A → T(PubMed:1905724)Curated
    Sequence conflicti327 – 3271A → G(PubMed:1900346)Curated
    Sequence conflicti327 – 3271A → G(PubMed:1905724)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53695 Genomic DNA. Translation: CAA37733.1.
    AP008231 Genomic DNA. Translation: BAD79071.1. Different initiation.
    PIRiS13326.
    RefSeqiYP_171591.2. NC_006576.1.

    Genome annotation databases

    EnsemblBacteriaiBAD79071; BAD79071; syc0881_c.
    GeneIDi3199069.
    KEGGisyc:syc0881_c.
    PATRICi32487518. VBISynElo117686_1027.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53695 Genomic DNA. Translation: CAA37733.1 .
    AP008231 Genomic DNA. Translation: BAD79071.1 . Different initiation.
    PIRi S13326.
    RefSeqi YP_171591.2. NC_006576.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GSA X-ray 2.40 A/B 2-433 [» ]
    3FQ7 X-ray 2.15 A/B 7-433 [» ]
    3FQ8 X-ray 2.00 A/B 7-433 [» ]
    3FQA X-ray 2.35 A/B 7-433 [» ]
    3GSB X-ray 3.00 A/B 2-433 [» ]
    4GSA X-ray 2.50 A/B 2-433 [» ]
    ProteinModelPortali P24630.
    SMRi P24630. Positions 7-433.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269084.syc0881_c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD79071 ; BAD79071 ; syc0881_c .
    GeneIDi 3199069.
    KEGGi syc:syc0881_c.
    PATRICi 32487518. VBISynElo117686_1027.

    Phylogenomic databases

    eggNOGi COG0001.
    HOGENOMi HOG000020210.
    KOi K01845.
    OrthoDBi EOG6QVRHN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    UPA00668 .
    BioCyci SELO269084:GCDQ-897-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P24630.

    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. "Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli."
      Grimm B., Bull A., Breu V.
      Mol. Gen. Genet. 225:1-10(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of Synechococcus. Deletion of a tripeptide close to the NH2 terminus and internal amino acid substitution."
      Grimm B., Smith A.J., Kannangara C.G., Smith M.
      J. Biol. Chem. 266:12495-12501(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
      Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
      Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
    4. "Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus."
      Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.
      Carlsberg Res. Commun. 54:67-79(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-17.
    5. "Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity."
      Hennig M., Grimm B., Contestabile R., John R.A., Jansonius J.N.
      Proc. Natl. Acad. Sci. U.S.A. 94:4866-4871(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiGSA_SYNP6
    AccessioniPrimary (citable) accession number: P24630
    Secondary accession number(s): Q5N3P9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 115 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing

    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

    External Data

    Dasty 3