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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Propionibacterium freudenreichii subsp. freudenreichii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL1), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL1)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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
OrganismiPropionibacterium freudenreichii subsp. freudenreichii
Taxonomic identifieri66712 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ06774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSDELFAE ALKVMPGGVS SPVRAYRSVG GTPRFVKRAL GSHIVDVDDK
60 70 80 90 100
RYVDLVCSWG PMIAGHAHPE VVAAVLQAVA DSTSFGAPSE VELRLAQAVV
110 120 130 140 150
ARMGGAIDKV RFTCSGTEAV MTAARLARGI TKRPLLVKFV GCYHGHSDSF
160 170 180 190 200
LVSAGSGVAS LGLPDSPGVP KEVAGDTVAL PYGRIDMVEE LFAERGDQVA
210 220 230 240 250
AIVTEGVPAN MGVIVPPEGF NRRLHDIAHA HGALLIQDEV LTGFRLSPTG
260 270 280 290 300
AWGLQGAKEG WTPDLFTFGK VIGGGMPLAA VGGSAQLMDY LAPEGPVYQA
310 320 330 340 350
GTLSGNPAAC AAGLATLALM DDAAYSRLDA TADRVSAMAD AALESAGVPH
360 370 380 390 400
RINKVSNLFS VFLTDAPVTD FASASKQDTK AFSRFFHAAL DAGLWLAPSG
410 420 430 440
FEAWFCSTAL DDDDLEVIDA GLHKAAQAAA QGLSSLEDVR R
Length:441
Mass (Da):45,932
Last modified:June 1, 1994 - v1
Checksum:i0F07395A67CAE4D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12643 Genomic DNA. Translation: BAA02164.1.
D85417 Genomic DNA. Translation: BAA21914.1.
PIRiA48959.
RefSeqiWP_044636331.1. NZ_CP010341.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12643 Genomic DNA. Translation: BAA02164.1.
D85417 Genomic DNA. Translation: BAA21914.1.
PIRiA48959.
RefSeqiWP_044636331.1. NZ_CP010341.1.

3D structure databases

ProteinModelPortaliQ06774.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

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]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of the gene encoding glutamate 1-semialdehyde 2,1-aminomutase, which is involved in delta-aminolevulinic acid synthesis in Propionibacterium freudenreichii."
    Murakami K., Hashimoto Y., Murooka Y.
    Appl. Environ. Microbiol. 59:347-350(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC 10470 / NRRL B-3523.

Entry informationi

Entry nameiGSA_PROFF
AccessioniPrimary (citable) accession number: Q06774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 22, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.