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Q04NV4 (GSA_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:LBJ_4011
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length441 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 – 441441Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382328

Amino acid modifications

Modified residue2791N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04NV4 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 0C21B4B10699304B

FASTA44148,001
        10         20         30         40         50         60 
MSQRSSELIS DSWKGSSSEE LFERAKIVSP GGVHSPVRSF RSVGGTPVFF VSANGATLTD 

        70         80         90        100        110        120 
VSGKEYVDFC LSFGPLILGH RDPEVEEVVR ETAGLAWSFG TAEPYSLELA EFITNRIPWA 

       130        140        150        160        170        180 
EKVRFVNSGT EAVMSALRVT RAATGREKIF KFDGCYHGHL DALLVKAGSG LAGESSSDSA 

       190        200        210        220        230        240 
GISSTAIANT LVLPLDDEMA VQKLFESEGK NIAALIIEPL PANYGLLVQR KEFLLKIVEI 

       250        260        270        280        290        300 
AKKYGTLVVF DEVISGFRTG FQGMSGLLGI RPDLVTYGKI IGGGFPVGCY AGRRDLLDLV 

       310        320        330        340        350        360 
APSGPVYQAG TLSANPFGMR AGLATLKKAE RDSIYSVLEV RTKTFADEMV KLLNGKTDQE 

       370        380        390        400        410        420 
WEAVTHSSLF WFRKKTQQAV RRIDQIPEGH KEGFAEVFHV LLKNGIYLAP SGYEVGFLSW 

       430        440 
AHNDSVIAKV LEIADKAFKE L 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000351 Genomic DNA. Translation: ABJ77416.1.
RefSeqYP_802174.1. NC_008511.1.

3D structure databases

ProteinModelPortalQ04NV4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_4011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ77416; ABJ77416; LBJ_4011.
GeneID4412234.
KEGGlbj:LBJ_4011.
PATRIC22362391. VBILepBor13265_3879.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAETRANGM.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-2993-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_LEPBJ
AccessionPrimary (citable) accession number: Q04NV4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 47 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