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Q1CUJ7 (GSA_HELPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:HPAG1_0308
OrganismHelicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]
Taxonomic identifier357544 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300920

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CUJ7 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: FA5B365A8B203795

FASTA43046,729
        10         20         30         40         50         60 
MELLHSINDF NEAKQVIAGG VNSPVRAFKS VKGTPPFILK GKGAYLYDVD NNHYIDFVQS 

        70         80         90        100        110        120 
WGPLIFGHAD EEIEENIINT LKKGTSFGAP TELETTLAKE IISCYEGLDK VRLVNSGTEA 

       130        140        150        160        170        180 
TMSAIRLARA YSQKDDLIKF EGCYHGHSDS LLVKAGSGCV TFGSPSSLGV PNDFSKHTLV 

       190        200        210        220        230        240 
ARYNDLNSTE ECFKKGNVGC VIIEPIAGNM GLVPAQKEFL LGLKALCEKY QAVLILDEVM 

       250        260        270        280        290        300 
SGFRASLSGS QEFYGVVPDL VTFGKVIGAG LPLACFGGRA EIMDLLSPIG GVYQAGTLSG 

       310        320        330        340        350        360 
NPLAVCAGLS ALYKIKRDKT LYTRLNALAI RLTQGLKKSA QSYNIALETL NRGSMFGFFF 

       370        380        390        400        410        420 
NENAVCDFDD ALKSDTEMFA KFHQKMLFKG VYLACSSFET GFICEPMTEE MIDLVVAKAD 

       430 
ESFDEIIKGV 

« Hide

References

[1]"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HPAG1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000241 Genomic DNA. Translation: ABF84375.1.
RefSeqYP_627049.1. NC_008086.1.

3D structure databases

ProteinModelPortalQ1CUJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357544.HPAG1_0308.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF84375; ABF84375; HPAG1_0308.
GeneID4098681.
KEGGhpa:HPAG1_0308.
PATRIC20601943. VBIHelPyl56048_0322.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMALMAHIAP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycHPYL357544:GH1F-317-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_HELPH
AccessionPrimary (citable) accession number: Q1CUJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 59 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