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B7IHH3 (GSA_THEAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:THA_1081
OrganismThermosipho africanus (strain TCF52B) [Complete proteome] [HAMAP]
Taxonomic identifier484019 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length423 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 – 423423Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382387

Amino acid modifications

Modified residue2591N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7IHH3 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 2E1E249686DE3C17

FASTA42346,921
        10         20         30         40         50         60 
MFEIAKKYMP GGVNSPVRAF KSVEMEPIFV KSAKKSKLID INNKEYIDYI QSWGALILGH 

        70         80         90        100        110        120 
AHEEVVEEIK KQAELGTSYG LCHELEVEMA RLIVKHIPSV EMVRMVNSGT EAVMSAIRLA 

       130        140        150        160        170        180 
RAYTNRELIV KFEGCYHGHS DGLLVKAGSG ALTFGTPSSK GVTEKIVSNT LVARYNDIES 

       190        200        210        220        230        240 
VKELFDKYGE NIACVIVEPV AGNMGVVLPK QGFLEGLREI TKEYGSLLIF DEVITGFRVS 

       250        260        270        280        290        300 
INGAQGYYNV FPDITTLGKI IGGGLPVGAY GGRKEIMELI SPQGPVYQAG TLSGNPLTLA 

       310        320        330        340        350        360 
AGIKTIKIIE NDPDFYSKLD ELGKYFEEGI VSALGDFDVK INRIKSMLSF FFSKQEVDSY 

       370        380        390        400        410        420 
EKVINSDVEI YKKLFKCLFE NGILLPPSPF ESLFISSSHT KEDIEKTVYY FEKFSKKLKE 


GKV 

« Hide

References

[1]"The genome of Thermosipho africanus TCF52B: lateral genetic connections to the Firmicutes and Archaea."
Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D., Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.
J. Bacteriol. 191:1974-1978(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TCF52B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001185 Genomic DNA. Translation: ACJ75537.1.
RefSeqYP_002334878.1. NC_011653.1.

3D structure databases

ProteinModelPortalB7IHH3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING484019.THA_1081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ75537; ACJ75537; THA_1081.
GeneID7070997.
KEGGtaf:THA_1081.
PATRIC23919166. VBITheAfr129358_1095.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHPLIIKT.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycTAFR484019:GJOH-1112-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_THEAB
AccessionPrimary (citable) accession number: B7IHH3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 43 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