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B8J3A3 (GSA_DESDA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:Ddes_2017
OrganismDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) [Complete proteome] [HAMAP]
Taxonomic identifier525146 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length423 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 – 423423Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382311

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8J3A3 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: D3B6943372710805

FASTA42345,286
        10         20         30         40         50         60 
MDTVSRQLFE KAQAVIPGGV NSPVRACHNV DSQPLFIAEA HGCHLTDVDG RQYIDFVLSW 

        70         80         90        100        110        120 
GPMILGHDEP SVTRAVCDAA HRGTSYGAPC PDEVLLAEAV VAAMPSLEMV RMVNSGTEAT 

       130        140        150        160        170        180 
MSALRLARAA TRRDKVLKFV GCYHGHADPF LAAAGSGLAT FSIPGTPGVP AAVVADTLLA 

       190        200        210        220        230        240 
PYNDLEAVKE CFARHGESIA AIIVEPVAAN MGLVLPKPGF LEGLRAICDQ YESLLIFDEV 

       250        260        270        280        290        300 
ITGFRAAFGG AQARFKVDPD LTTFGKIIGG GLPVGAFGGK RRYMELIAPR GGVYQAGTLS 

       310        320        330        340        350        360 
GNPLAMAAGL ATLGILRKAD YDGLENRTRA FAYSMRDIIA AKGVPLQMPT LASMFCPYFS 

       370        380        390        400        410        420 
EHEVTDFADA QKCDQKLFTS FYKQMRAQGI YLAPSGYETG MVSFAHTDED FNRALDAARK 


VMF 

« Hide

References

[1]"Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Hazen T.C.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27774 / DSM 6949.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001358 Genomic DNA. Translation: ACL49913.1.
RefSeqYP_002480591.1. NC_011883.1.

3D structure databases

ProteinModelPortalB8J3A3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING525146.Ddes_2017.

Proteomic databases

PRIDEB8J3A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL49913; ACL49913; Ddes_2017.
GeneID7285733.
KEGGdds:Ddes_2017.
PATRIC21738046. VBIDesDes50650_2355.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycDDES525146:GIWF-2083-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_DESDA
AccessionPrimary (citable) accession number: B8J3A3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 37 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