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A1WMA0 (GSA_VEREI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Veis_3024
OrganismVerminephrobacter eiseniae (strain EF01-2) [Complete proteome] [HAMAP]
Taxonomic identifier391735 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter

Protein attributes

Sequence length437 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 – 437437Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300957

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WMA0 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: FA3D2C2FFABA6754

FASTA43746,110
        10         20         30         40         50         60 
MTPNTDLNIP LFERAKALIP GGVNSPVRAF KAVGGTPRFV KRARGAYFWD ANDQRFIDYI 

        70         80         90        100        110        120 
GSWGPMILGH GHPAVLEAVQ QAALEGLSFG APTERELELA EAILRLLPSM QMIRLVSSGT 

       130        140        150        160        170        180 
EAGMSAIRLA RGATGRSKLI KFEGCYHGHA DALLVKAGSG LATFGNATSA GVPAEVVQHT 

       190        200        210        220        230        240 
LVLEYNSIEQ LERAFALHGK ELACLIIEPI AGNMNLVRAS VPFMRRCREL CSEYGALLVL 

       250        260        270        280        290        300 
DEVMTGFRVA PGGAQSLYAR DIPGFQPDLT VLGKVIGGGM PLAAFGGSRA LMEHLAPLGA 

       310        320        330        340        350        360 
VYQAGTLSGN PVATACGLAT LRAIGQPGFF AALSARTRAL VEGLRGAAAA EGVAFSADSE 

       370        380        390        400        410        420 
GGMFGFFLLP ALPRNYAQVL QTDSARFNQL FHGLLERGIY IAPALYEAGF VSAAHSDEDI 

       430 
AATVAAAREV FKTLAKP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EF01-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000542 Genomic DNA. Translation: ABM58757.1.
RefSeqYP_997775.1. NC_008786.1.

3D structure databases

ProteinModelPortalA1WMA0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391735.Veis_3024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM58757; ABM58757; Veis_3024.
GeneID4694901.
KEGGvei:Veis_3024.
PATRIC24019803. VBIVerEis120356_3288.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycVEIS391735:GHY5-3056-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.
ProtoNetSearch...

Entry information

Entry nameGSA_VEREI
AccessionPrimary (citable) accession number: A1WMA0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 50 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