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A9BY74 (GSA_DELAS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:Daci_1569
OrganismDelftia acidovorans (strain DSM 14801 / SPH-1) [Complete proteome] [HAMAP]
Taxonomic identifier398578 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeDelftia

Protein attributes

Sequence length438 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 – 438438Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382304

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BY74 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: A4FBE794778D0CBE

FASTA43846,977
        10         20         30         40         50         60 
MADSCTMTTD LNIPLFERAK AVIPGGVNSP VRAFNAVGGT PRFVRRAQGA HFWDENAQQF 

        70         80         90        100        110        120 
TDYIGSWGPM ILGHGHPEVM AAVQAAALEG FSFGAPTERE VVLAEKILSL MPSMDMVRMV 

       130        140        150        160        170        180 
SSGTEAGMSA LRLARGFTGR NKIIKFNGCY HGHADALLVK AGSGLATFGA SSSAGVPQDV 

       190        200        210        220        230        240 
VKDTVVLEYN DVGQLEEAFA QFGDQIACVI MEPIAGNMNF VRASVPFTRR IRELTREHGA 

       250        260        270        280        290        300 
LMVYDEVMTG FRVALGSAQS LYAQHIEGFA PDITVLGKVI GGGMPMAAFG ARREIMEKLS 

       310        320        330        340        350        360 
PLGPVYQAGT LSGNPIATAC GLKTLELISE PGFHDALHAK TGRLMAGFKA EADAAGVPFS 

       370        380        390        400        410        420 
VDHQGGLFGF YLLPELPSTW TEVMKTDGAR FNRFFHGMLE RGHYFAPALY EAGFVSAAHT 

       430 
DADIDKTIEA AREVFKTL 

« Hide

References

[1]"Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14801 / SPH-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000884 Genomic DNA. Translation: ABX34213.1.
RefSeqYP_001562598.1. NC_010002.1.

3D structure databases

ProteinModelPortalA9BY74.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398578.Daci_1569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX34213; ABX34213; Daci_1569.
GeneID5747126.
KEGGdac:Daci_1569.
PATRIC21637049. VBIDelAci41351_1610.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycDACI398578:GHK3-1590-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_DELAS
AccessionPrimary (citable) accession number: A9BY74
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 56 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