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B9L0Q2 (GSA_THERP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:trd_1123
OrganismThermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2) [Complete proteome] [HAMAP]
Taxonomic identifier309801 [NCBI]
Taxonomic lineageBacteriaChloroflexiThermomicrobialesThermomicrobiaceaeThermomicrobium

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201036

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B9L0Q2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: D567EB4C01C5E732

FASTA43045,749
        10         20         30         40         50         60 
MMMENSGSLW DAARQFFPGG VNSPVRAFRA VGEEPVVAVR GEGAYLIDAD GRRFLDYICS 

        70         80         90        100        110        120 
WGALLAGHAH PHVVDRLSEA IQRGTSFGLL SPYEVELARA IVASVPAIEL VRFVNSGTEA 

       130        140        150        160        170        180 
TMSAIRLARA VTGRNLVVKF AGCYHGHVDG LLVAAGSGVL TFGLPGTPGV TEGTARDTLV 

       190        200        210        220        230        240 
LPYNDQEAVE DAFAQHGERI AAVIVEPVAG NMGVVPPAAG FLSRLRELTR QAGALLIFDE 

       250        260        270        280        290        300 
VITGFRLGLG GAQERFGILP DLTCLGKVIG GGLPVGAYGG RRDLMEQVAP NGPVYQAGTL 

       310        320        330        340        350        360 
AGNPLSMVAG LATLELAREP GVYGRLETLA AWLQRGLEET IQESGLPAHV QRVGSMLTLF 

       370        380        390        400        410        420 
FSQQPVTDAQ TAERCDTARF AAFHRAMRAQ GILLPPSQFE AWFVSLAHRE EDIDRTIEAA 

       430 
RKALAEVARG 

« Hide

References

[1]"Complete genome sequence of the aerobic CO-oxidizing thermophile Thermomicrobium roseum."
Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L., Eisen J.A.
PLoS ONE 4:E4207-E4207(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27502 / DSM 5159 / P-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001275 Genomic DNA. Translation: ACM05709.1.
RefSeqYP_002522332.1. NC_011959.1.

3D structure databases

ProteinModelPortalB9L0Q2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309801.trd_1123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM05709; ACM05709; trd_1123.
GeneID7355638.
KEGGtro:trd_1123.
PATRIC23913418. VBITheRos91376_1059.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMASQFETIF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycTROS309801:GI0S-1111-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_THERP
AccessionPrimary (citable) accession number: B9L0Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 41 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