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Q5E2W6 (GSA_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:VF_2135
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length431 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 – 431431Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120464

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E2W6 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: AC2C04C6A0B46FFF

FASTA43145,935
        10         20         30         40         50         60 
MTKSAELFAK AQDKIPGGVN SPVRAFAGVG GSPIFVERAD GPLIFDADGK AYIDYVGSWG 

        70         80         90        100        110        120 
PMILGHNHAA IREAVISAAQ RGLSFGAPTE TEITMAELVS ELVPSMEQVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRDKIMKFEG CYHGHADSLL VKAGSGALTL GQPSSPGVPA DFAKYTLTAT 

       190        200        210        220        230        240 
FNDLDSVREL FAVNKGEIAC IIVEPVAGNM NCIPPVEGFH EGLRQICDEE GALLIFDEVM 

       250        260        270        280        290        300 
TGFRVAENCA QGYYNIKPDL TTLGKVIGGG MPVGAFGGRK EVMQYIAPTG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGFA CLKVLTEEGN EKRLADTTRH LANGFKELAN KHGIPMVVNQ VGGMFGFFFT 

       370        380        390        400        410        420 
DQETVTSYAD VAKCDIERFK RFFHLMLKKG VYLAPSAFEA SFTSLAHGPK EIEATLEAAD 

       430 
QCFAIIASEA K 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW86630.1.
RefSeqYP_205518.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E2W6.
SMRQ5E2W6. Positions 2-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_2135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW86630; AAW86630; VF_2135.
GeneID3279385.
KEGGvfi:VF_2135.
PATRIC20115002. VBIVibFis127983_2177.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycAFIS312309:GIWP-2253-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_VIBF1
AccessionPrimary (citable) accession number: Q5E2W6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 15, 2005
Last modified: May 14, 2014
This is version 70 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