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Q67KM3 (GSA_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:STH2790
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length433 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 – 433433Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243626

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67KM3 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: EB1021B9102E297C

FASTA43345,940
        10         20         30         40         50         60 
MTARYERSAA LYERAVARIV GGVNSPARSF KSVGGGAPVF MARGQGPYLY DVDGNRYIDY 

        70         80         90        100        110        120 
IGAFGAGMFG HGHPELVAAV ARAAEGGTIY GTPNPWEVEL AERIHQALPS MERIRFVTTG 

       130        140        150        160        170        180 
TEAVMSAVRV ARAFTGRPKI IKMEGCYHGH SDFALIAAGS GPSQLGTPDS AGVTEGVAQD 

       190        200        210        220        230        240 
VITVPYNDLD SLGEALDVWG PQVAAVLVEP IVGNFGVAMP KPGYLEGVKR LAHAHGALLI 

       250        260        270        280        290        300 
FDEVITGFRV AYGGAQTLLG IEPDLTTLGK IIGGGLPLAA YGGRAEIMDW VAPLGPAYQA 

       310        320        330        340        350        360 
GTLAGNPLCM QVALTGLEIL SRPGVYERLD ADAAYLADGL VRSARSHGHT VQLGRAGSMF 

       370        380        390        400        410        420 
TLFFCDEPVV DYRTAQRSDP AKFAAMFRGL LDRGIALAPS RFEAWMLTVQ HTRADLEETL 

       430 
QIADEVFAQM AGQ 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD41775.1.
RefSeqYP_076619.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67KM3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH2790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD41775; BAD41775; STH2790.
GeneID2982017.
KEGGsth:STH2790.
PATRIC23783759. VBISymThe116959_2770.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAPVVMERA.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-2889-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_SYMTH
AccessionPrimary (citable) accession number: Q67KM3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 73 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