Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5SJS4 (GSA_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:TTHA0934
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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 – 424424Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243636

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

............................................................................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SJS4 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8134C11065EEFF77

FASTA42446,034
        10         20         30         40         50         60 
MERPISEAYF QEAKRHIPGG VSSPVRAFKA VGGTPPFLVR GEGAYVWDAD GNRYLDYVMS 

        70         80         90        100        110        120 
WGPLILGHAH PKVLARVRET LERGLTFGAP SPLEVALAKK VKRAYPFVDL VRFVNSGTEA 

       130        140        150        160        170        180 
TMSALRLARG YTGRPYIVKF RGNYHGHADG LLVEAGSGAL TLGVPSSAGV PEEYAKLTLV 

       190        200        210        220        230        240 
LEYNDPEGLR EVLKRRGEEI AAIIFEPVVG NAGVLVPTED FLKALHEAKA YGVLLIADEV 

       250        260        270        280        290        300 
MTGFRLAFGG ATELLGLKPD LVTLGKILGG GLPAAAYAGR REIMEKVAPL GPVYQAGTLS 

       310        320        330        340        350        360 
GNPLAMAAGL ATLELLEENP GYYAYLEDLG ARLEAGLKEV LKEKGLPHTV NRVGSMITVF 

       370        380        390        400        410        420 
FTEGPVVTFQ DARRTDTELF KRFFHGLLDR GIYWPPSNFE AAFLSVAHRE EDVEKTLEAL 


RKAL 

« Hide

References

[1]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD70757.1.
RefSeqYP_144200.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7UX-ray1.90A1-424[»]
ProteinModelPortalQ5SJS4.
SMRQ5SJS4. Positions 1-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA0934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70757; BAD70757; BAD70757.
GeneID3168378.
KEGGttj:TTHA0934.
PATRIC23956832. VBITheThe93045_0917.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.
PhylomeDBQ5SJS4.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-965-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...

Other

EvolutionaryTraceQ5SJS4.

Entry information

Entry nameGSA_THET8
AccessionPrimary (citable) accession number: Q5SJS4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 71 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways