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A5VM65 (GSA_LACRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:Lreu_1700
OrganismLactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]
Taxonomic identifier557436 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

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
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_0000382324

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VM65 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 8B831E94962EF36C

FASTA43146,682
        10         20         30         40         50         60 
MSKLDTTKSK IAFKEAQKYM PGGVNSPVRA FKNVGGDPLF IDHGKDEYIY DIDGNKYIDY 

        70         80         90        100        110        120 
VLSWGPLILG HADDHVVAEL DKAVAKGTSY GAPTLQETEL AKIVNKIMPS IEMIRMVSSG 

       130        140        150        160        170        180 
TEATMSAIRL ARGYTHRKKI VKFVGNYHGH SDSLLVDAGS GLATFGINTS PGVPDDLAYD 

       190        200        210        220        230        240 
TLTVAYNDVA GVKKLFAEHG DEIACAIVEP VAGNMGVIPG TQEFLQTLRN VTNEHGALLI 

       250        260        270        280        290        300 
FDEVMSGFRA AYHGVQSLVN ITPDLTTLGK VIGGGLPVGA FGGRREIMEN ITPAGDIYHA 

       310        320        330        340        350        360 
GTLSGNPLAM TGGISTLEQL TPDDYVEMDK KVTALTEGIK HAADQYGVPM TVHHVGTMWS 

       370        380        390        400        410        420 
YFYNSDPINN FDDVKACDQK LFEKCFWELL AHGVYVAPSQ FETNFISTKH TDEDIEKTIA 

       430 
AFDAAFNAAT K 

« Hide

References

[1]"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri."
Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. expand/collapse author list , Ivanova N., Kyrpides N.C., Walter J.
PLoS Genet. 7:E1001314-E1001314(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 20016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000705 Genomic DNA. Translation: ABQ83939.1.
RefSeqYP_001272276.1. NC_009513.1.

3D structure databases

ProteinModelPortalA5VM65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557436.Lreu_1700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ83939; ABQ83939; Lreu_1700.
GeneID5188957.
KEGGlre:Lreu_1700.
PATRIC22256661. VBILacReu87937_1718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLREU557436:GC7Y-1783-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_LACRD
AccessionPrimary (citable) accession number: A5VM65
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 63 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