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Q8RFY7 (GSA_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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:FN0540
OrganismFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]
Taxonomic identifier190304 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

Protein attributes

Sequence length434 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 – 434434Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120412

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RFY7 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 1FE9C6BD0A95A58A

FASTA43447,773
        10         20         30         40         50         60 
MVFKNSIDLY KKAVELIPGG VNSPVRAFKS VNREAPIFIK KGQGAKIWDE DDNEYIDYIC 

        70         80         90        100        110        120 
SWGPLILGHN HPKVIEEVKK IIENGSSYGL PTKYEVDLAE LIVDIVPSIE KVRLTTSGTE 

       130        140        150        160        170        180 
ATMSAVRLAR AYTQRNKILK FEGCYHGHSD ALLVKSGSGL LTEGYQDSNG ITDGVLKDTL 

       190        200        210        220        230        240 
TLPFGDIEKV KEILKNKDVA CVIVEPIPAN MGLIETHKEF LQGLGKVTEK TGTILIFDEV 

       250        260        270        280        290        300 
ISGFRLALGG AQEFFGITPD LTTLGKIIGG GYPVGAFGGK KEIMDLVAPV GRVYHAGTLS 

       310        320        330        340        350        360 
GNPIASKAGF ATISYLKENP NIYKELEEKT NYLIDNIEIL AKKYSVNVCV NSMGSLFTIF 

       370        380        390        400        410        420 
FVDIDKVENL EDSLKSNTEN FSIYFNTMLE NGIVIPPSQF EAHFLSMAHT KKELNRTLEV 

       430 
IEMAFKKIGE KSGK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009951 Genomic DNA. Translation: AAL94736.1.
RefSeqNP_603437.1. NC_003454.1.

3D structure databases

ProteinModelPortalQ8RFY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190304.FN0540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL94736; AAL94736; FN0540.
GeneID992835.
KEGGfnu:FN0540.
PATRIC21950849. VBIFusNuc122357_1107.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

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_FUSNN
AccessionPrimary (citable) accession number: Q8RFY7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 85 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