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A3DIF3 (GSA_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Cthe_2530
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000059984

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3DIF3 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: A91AAE58A0A0914C

FASTA42745,932
        10         20         30         40         50         60 
MTLSKSKLLF ERAKKVIPGG VNSPVRAFGA VGGYPPFIKK AKGARIYDAD GNEYIDYVGS 

        70         80         90        100        110        120 
WGPMILGHSH PRVLEAVSKT MVDGLSFGAA TELEVQMAEL ITELVPSVEM VRMVNSGTEA 

       130        140        150        160        170        180 
VMSAIRVARG YTKREKIIKF AGCYHGHADS MLVKVGSGAM TNGIPNSGGV TAGAAKDTLI 

       190        200        210        220        230        240 
ARYNDIDSVK LLFEQNKGNI AAVIVEPVAA NMGVVPPKDN FLEELRKLCD KEEALLIFDE 

       250        260        270        280        290        300 
VITGFRLAIG GAQQYFGVNA DLVTYGKIIG GGMPVGAYGG RREIMECVAP VGDVYQAGTL 

       310        320        330        340        350        360 
SGNPIAMSAG IATLRELYEN PGIFENINRL GQRLSEGLGK ITKYTVKAVG SLVCVFMTEE 

       370        380        390        400        410        420 
EVNDYDSAVK SDTGLFGRYF NHLLNNGIYI APSQFEAMFV SNAHTDKDID ETLEKVSLFF 


ARKSPPA 

« Hide

References

[1]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000568 Genomic DNA. Translation: ABN53732.1.
RefSeqYP_001038925.1. NC_009012.1.

3D structure databases

ProteinModelPortalA3DIF3.
SMRA3DIF3. Positions 1-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_2530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN53732; ABN53732; Cthe_2530.
GeneID4809286.
KEGGcth:Cthe_2530.
PATRIC19519068. VBICloThe47081_2693.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMASQFETIF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-2618-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_CLOTH
AccessionPrimary (citable) accession number: A3DIF3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 54 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