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Q0VSP6 (GSA_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:ABO_0354
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax

Protein attributes

Sequence length426 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382246

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VSP6 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 7748B8D4B9908256

FASTA42644,870
        10         20         30         40         50         60 
MPRKHSEQLF RQAQKHIPGG VNSPVRAFKS VGGTPVFFHS ARGAHLFDED DNKYIDYVGS 

        70         80         90        100        110        120 
WGPMILGHNH PHVVAAVQAA VEQGLSFGAP TATEVAMADK VCELVPSMDM VRMVNSGTEA 

       130        140        150        160        170        180 
TMSAIRLARG YTGRNKIIKF EGCYHGHVDS LLVKAGSGAI AIPGSPGVPE AVTADTLVLD 

       190        200        210        220        230        240 
YNDAASVTQA FKEHGDDIAA VIVEPVAGNM NCVPATENFL QTLRQQCDDN GAVLIFDEVM 

       250        260        270        280        290        300 
SGFRVALGGA QGHYGITPDM TTLGKIVGGG MPVGAFGGKQ AIMEHLAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGLA TLNLISEPGF HQALAEKTTR LLEGLTAAAH AEGVAFTTAQ AGAMFGLFFT 

       370        380        390        400        410        420 
DQNRISSFTE VMACDSERFN RFFHAMLDQG IYLAPSAFEA GFVSAAHSND DIDATITAAR 


KAFGKI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286690 Genomic DNA. Translation: CAL15802.1.
RefSeqYP_692074.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VSP6.
SMRQ0VSP6. Positions 1-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393595.ABO_0354.

Proteomic databases

PRIDEQ0VSP6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL15802; CAL15802; ABO_0354.
GeneID4212189.
KEGGabo:ABO_0354.
PATRIC20838319. VBIAlcBor124741_0375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycABOR393595:GHRI-356-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_ALCBS
AccessionPrimary (citable) accession number: Q0VSP6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 65 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