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Q725I1 (GSA_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:DVU_3168
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]
Taxonomic identifier882 [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
Reference 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_0000243570

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q725I1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3587A9C3DB05C3F2

FASTA42344,469
        10         20         30         40         50         60 
MSQRSSELFE RAQQLIPGGV NSPVRACLGV DSEPLFIARA AGSRLHTVDG ETFIDFVESW 

        70         80         90        100        110        120 
GPMLLGHTHP EVTAAVHAAV DRGTSYGAPC EDEVVLAAKV VDALPGVDMV RMVNSGTEAT 

       130        140        150        160        170        180 
MSALRLARGY TGRTKLVKFV GCYHGHADPF LASAGSGVAT LSIPGTPGVP ESTVRDTLLA 

       190        200        210        220        230        240 
PYNDLAAVKD LFALHGKDIA AIIVEAVAGN MGLVPPKAGF LEGLRELCDQ HGALLIFDEV 

       250        260        270        280        290        300 
ITGFRVSFGG AQQRFGITPD LTTLGKIIGG GLPVGAYGGK REIMQRIAPC GEVYQAGTLS 

       310        320        330        340        350        360 
GNPLAMAAGI ATLDVLSRSD YAGLEARVAA FVKELEAILK GKGVPVRINT LASMFTVFFT 

       370        380        390        400        410        420 
NDPVTDFASA KTADGALYTS FYKQMRAQGI YLAPSPFEAA MVSFAHTDDD LAAMLDAARK 


VTF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017285 Genomic DNA. Translation: AAS97638.1.
RefSeqYP_012378.1. NC_002937.3.

3D structure databases

ProteinModelPortalQ725I1.
SMRQ725I1. Positions 2-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING882.DVU3168.

Proteomic databases

PRIDEQ725I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS97638; AAS97638; DVU_3168.
GeneID2795873.
KEGGdvu:DVU3168.
PATRIC32065878. VBIDesVul119526_2873.

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycDVUL882:GJIL-3251-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_DESVH
AccessionPrimary (citable) accession number: Q725I1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 74 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