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B8DHJ5 (GSA2_LISMH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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 2

Short name=GSA 2
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name=GSA-AT 2
Gene names
Name:hemL2
Ordered Locus Names:LMHCC_1016
OrganismListeria monocytogenes serotype 4a (strain HCC23) [Complete proteome] [HAMAP]
Taxonomic identifier552536 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length429 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382333

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8DHJ5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 02AD16E4E8FF2E30

FASTA42946,561
        10         20         30         40         50         60 
MQIYSKSEKA FKEAKKVLPG GVNSPVRAFN SVDASPVFMD HGKGAYITDI DGNEYIDYVL 

        70         80         90        100        110        120 
SWGPLILGHA NPSVVQAITN AAMKGTSFGT PTEIETELAK LVIERVPSIE IVRMVSSGTE 

       130        140        150        160        170        180 
ATMSAIRLAR GYTKREKILK FEGSYHGHGD SLLIKAGSGV ATLGLPDSPG VTKGLAADTI 

       190        200        210        220        230        240 
TVPYNDIEGA KLAFEKYGEE IAAVIVEPVA GNMGVVPPIE GFLEGLRELT TNYGSLLIFD 

       250        260        270        280        290        300 
EVMTGFRVDY YSAQGYYVVT PDLTCLGKVI GGGLPVGAYG GKKEIMEQIA PAGSIYQAGT 

       310        320        330        340        350        360 
LSGNPLAMNA GFETVRQLTP QDYDVFRTLI KRMEEGLTEI SARRQVPLSI NKAGSMFGFF 

       370        380        390        400        410        420 
FTDQKVTNFD TAKTSDLEFF RSYYREMLGQ GIFLPPSQFE GVFISTMHTE KEIDKTLDAF 


DTTCKILRG 

« Hide

References

[1]"Genome sequence of lineage III Listeria monocytogenes strain HCC23."
Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M., Lawrence M.L.
J. Bacteriol. 193:3679-3680(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HCC23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001175 Genomic DNA. Translation: ACK39364.1.
RefSeqYP_002349978.1. NC_011660.1.

3D structure databases

ProteinModelPortalB8DHJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING552536.LMHCC_1016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK39364; ACK39364; LMHCC_1016.
GeneID7079949.
KEGGlmh:LMHCC_1016.
PATRIC20317149. VBILisMon86872_1005.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLMON552536:GIW4-1052-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 nameGSA2_LISMH
AccessionPrimary (citable) accession number: B8DHJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 40 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