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A5EXX1 (GSA_DICNV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:DNO_1024
OrganismDichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]
Taxonomic identifier246195 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

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_0000382312

Amino acid modifications

Modified residue2631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EXX1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 1D52061B62ADC0DE

FASTA42645,210
        10         20         30         40         50         60 
MTDSAFTRAA RVIPGGVNSP VRAFKSVGGE PIFIARAEGA YLYDVNGRRY IDYVGSYGPM 

        70         80         90        100        110        120 
INGHAHPEIV AAVCRASRNG MSYGAPNELE TELAEKIVAR VPSVEMVRMC NSGTEATMSA 

       130        140        150        160        170        180 
IRLARAATNR TQILKFAGCY HGHSDALLVS AGSGALTFGS PNSPGVPEDF VRHTLTAPYN 

       190        200        210        220        230        240 
DIAALERIFV QHGKNLAAVI VEPIAGNMNC VPPLPEFLPT LRALTKKYGV ILIIDEVMTG 

       250        260        270        280        290        300 
FRVAYAGAQG LYDIAADLTT FGKVIGGGMP VGAFAGSADL MSMLSPVGSV YQAGTLSGNP 

       310        320        330        340        350        360 
VAMIAGITNL RLTEAEGFYD TLAAKTQKLA EGLRQAAKKN GIHVVVNDVC GMLGLFFTDL 

       370        380        390        400        410        420 
PQVCNFADVQ TADTARFAKF FHAMLAEGVN LAPSAYETIF VSMAHDDAVL DETIAIAEYV 


FAHLEE 

« Hide

References

[1]"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus."
Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. expand/collapse author list , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T.
Nat. Biotechnol. 25:569-575(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCS1703A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000513 Genomic DNA. Translation: ABQ14353.1.
RefSeqYP_001209912.1. NC_009446.1.

3D structure databases

ProteinModelPortalA5EXX1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246195.DNO_1024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ14353; ABQ14353; DNO_1024.
GeneID5123090.
KEGGdno:DNO_1024.
PATRIC21786388. VBIDicNod48475_1022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycDNOD246195:GHHS-1021-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_DICNV
AccessionPrimary (citable) accession number: A5EXX1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 57 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