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A6T2A2 (GSA_JANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:mma_2959
OrganismJanthinobacterium sp. (strain Marseille) (Minibacterium massiliensis) [Complete proteome] [HAMAP]
Taxonomic identifier375286 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeJanthinobacterium

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000059992

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6T2A2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 6505BCA1A7624AD7

FASTA43245,682
        10         20         30         40         50         60 
MSSKNDQLFA RAQLSTPGGV NSPVRAFRSV GGTPRFITKA EGPYFWDADD RRYIDYIGSW 

        70         80         90        100        110        120 
GPAIVGHAHP DVVKAVQDAA TRGLSFGAPT EAEIEMAELI CRLVPSIEQV RLVSSGTEAA 

       130        140        150        160        170        180 
MSALRLARGA TGRDKIIKFE GCYHGHADSL LVKAGSGLLT FGNPTSAGVP EDFAKHTLVL 

       190        200        210        220        230        240 
DYNDPAQLEN VFKEMGDSIA CVIVEPVAGN MNLLPATPEF LQTMRRVCTQ YGAVMILDEV 

       250        260        270        280        290        300 
MSGFRVALGG AQSLYGITPD LTVLGKVIGG GLPVAAFGGR ADIMRHLAPL GGVYQAGTLS 

       310        320        330        340        350        360 
GNPVTVAAGM ATLKLIQAPG FYENLTAQTT KLVHGFSAAA READIAFCAN SVGGMFGLYF 

       370        380        390        400        410        420 
ASEVPVSYDT MMKCDKTRFN AFFHAMLDAG VYLAPSAFEA GFVSAQHDDA VIDSSIKAAR 

       430 
AAFAQLADDC DD 

« Hide

References

[1]"Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria."
Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Marseille.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000269 Genomic DNA. Translation: ABR88327.1.
RefSeqYP_001354649.1. NC_009659.1.

3D structure databases

ProteinModelPortalA6T2A2.
SMRA6T2A2. Positions 3-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375286.mma_2959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR88327; ABR88327; mma_2959.
GeneID5353256.
KEGGmms:mma_2959.
PATRIC22158439. VBIJanSp106498_2982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycJSP375286:GJ8U-3004-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 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]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_JANMA
AccessionPrimary (citable) accession number: A6T2A2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways