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B0SNK3 (GSA_LEPBP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:LEPBI_I1168
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris) [Complete proteome] [HAMAP]
Taxonomic identifier456481 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length425 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 – 425425Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382327

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SNK3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 261C16644B7312E1

FASTA42546,412
        10         20         30         40         50         60 
MNSETLFQRS KQVVPGGVHS PVRSFSSVGG TPIFFSEARG AYLKSVEGND FIDYCLSFGP 

        70         80         90        100        110        120 
LLFGHRHPEI QEVVEDTVNK AWSFGACEPY SLELAEFITE RIPWVEKIRF VNSGTEAVMS 

       130        140        150        160        170        180 
ALRVARAATG RNKILKFDGC YHGHLDQLLV KSGSGLAGLS SSDSKGIGPE IIQNTLVLPL 

       190        200        210        220        230        240 
DDESKLEELF QREGSNIACL AIEPLPANYG LLPQRIEFLK KCRELTTKYG VLLLFDEVIS 

       250        260        270        280        290        300 
GFRVSFQGMA GITGIIPDLV CYGKIIGGGF PVGAYAGKRE LMDLVAPSGP VYQAGTLSAN 

       310        320        330        340        350        360 
PIGMRAGLKT LTKAWTENPY PALESATKQL TDGILTLLSE KGDTNWEAVT FGSLFWLKGK 

       370        380        390        400        410        420 
TENPIRRIDQ IPGTHKSNFA TLFHKLLKQG VYLAPSGYEV GFLSTAHTND IINLTLEKTK 


KALKD 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / ATCC 23582 / Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000786 Genomic DNA. Translation: ABZ97284.1.
RefSeqYP_001838560.1. NC_010602.1.

3D structure databases

ProteinModelPortalB0SNK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING456481.LEPBI_I1168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ97284; ABZ97284; LEPBI_I1168.
GeneID6222448.
KEGGlbi:LEPBI_I1168.
PATRIC22349092. VBILepBif123590_1189.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycLBIF456481:GCM0-1152-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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_LEPBP
AccessionPrimary (citable) accession number: B0SNK3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 43 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