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B2USD7 (GSA_HELPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:HPSH_01585
OrganismHelicobacter pylori (strain Shi470) [Complete proteome] [HAMAP]
Taxonomic identifier512562 [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_1000121896

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2USD7 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: CFC51794A76E828B

FASTA43046,684
        10         20         30         40         50         60 
MELLHSINDF NEAKQVIAGG VNSPVRAFKS VKGTPPFILK GKGAYLYDVD NNHYIDFVQS 

        70         80         90        100        110        120 
WGPLIFGHAD EEIEENIINV LKKGTSFGTP TELETTLAKE IISCYEGLDK VRLVSSGTEA 

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

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

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

       310        320        330        340        350        360 
NPLAVCAGLS ALYKIKRDKT LYTRLNALAV RLAQGLKKSA QSYNIALETL NRGSMFGFFF 

       370        380        390        400        410        420 
NENAVRDFDD ALKSDTEMFA KFHQKMLFKG VYLACSSFET GFICEPMTEE MIDLAVAKAD 

       430 
ESFDEIIKGV 

« Hide

References

[1]"Genome sequence of Helicobacter pylori from the remote Amazon: traces of Asian ancestry of the first Americans."
Kersulyte D., Kalia A., Gilman R.H., Berg D.E.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Shi470.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001072 Genomic DNA. Translation: ACD47769.1.
RefSeqYP_001909799.1. NC_010698.2.

3D structure databases

ProteinModelPortalB2USD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING512562.HPSH_01585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD47769; ACD47769; HPSH_01585.
GeneID6297135.
KEGGhps:HPSH_01585.
PATRIC20611981. VBIHelPyl23559_0306.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHPYL512562:GHHZ-316-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_HELPS
AccessionPrimary (citable) accession number: B2USD7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 45 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