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B5EFG4 (GSA_GEOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:Gbem_3927
OrganismGeobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622) [Complete proteome] [HAMAP]
Taxonomic identifier404380 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

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_1000121891

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B5EFG4 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: B87B06FA6D41E66E

FASTA42744,879
        10         20         30         40         50         60 
MQNSRSTKLF QQALQSIPGG VNSPVRAFRS VGSDPLFIKK AAGPRIYDED GNAFIDYVGS 

        70         80         90        100        110        120 
WGPMILGHCH PQVVSAIKAA VDNGASFGAP TELEITLAEM VIDAVPSIEM VRMVSSGTEA 

       130        140        150        160        170        180 
TMSAIRLARG YTGRDNILKF SGCYHGHSDS LLVKAGSGAA TFGVPDSPGV PADLAKHTLT 

       190        200        210        220        230        240 
ATYNDLDSVR ALVAANKGSI ACIIVEPVAG NMGTVPPKEG FLEGLRSICS EEGIVLIFDE 

       250        260        270        280        290        300 
VMSGFRVAYG GVQELYGVTP DMTTLGKIIG GGLPVGAFGG KKEIMSLLSP AGGVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMTAG IETLKLLKQP GFYQKLEEKS AFVAEGIAKA AKDAGFPIYS TRVGSMFCAF 

       370        380        390        400        410        420 
FSKDPVYDWD SAAKCDTKAF AAYFKAMLNE GIYLAPSQFE TAFVGISHST EDLEQTIAAA 


AKCFKAL 

« Hide

References

[1]"Complete sequence of Geobacter bemidjiensis BEM."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Lovley D., Richardson P.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bem / ATCC BAA-1014 / DSM 16622.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001124 Genomic DNA. Translation: ACH40919.1.
RefSeqYP_002140715.1. NC_011146.1.

3D structure databases

ProteinModelPortalB5EFG4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING404380.Gbem_3927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH40919; ACH40919; Gbem_3927.
GeneID6780791.
KEGGgbm:Gbem_3927.
PATRIC21991472. VBIGeoBem56306_3837.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAAKHTIVL.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycGBEM404380:GHFR-3993-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_GEOBB
AccessionPrimary (citable) accession number: B5EFG4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 14, 2008
Last modified: May 14, 2014
This is version 44 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