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Q7VHK3 (GSA_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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:HH_0964
OrganismHelicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]
Taxonomic identifier235279 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length435 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 – 435435Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120413

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VHK3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B899B67ECD723139

FASTA43546,959
        10         20         30         40         50         60 
MDILQSINDF NEAKQVIPGG VNSPVRAFGS VGGTPRFIAK GKGAYIYDED DNEYIDFVQS 

        70         80         90        100        110        120 
WGPLIFGHAN EVIESALSLA IKDGLSFGAP TEKETTLVKQ IIALSGSAEK MRLVNSGTEA 

       130        140        150        160        170        180 
TMSALRLARA YSNKDDIIKF EGCYHGHSDS LLVSAGSGCA TFGTPSSPGV PNDITKHTLV 

       190        200        210        220        230        240 
ARYNDIESVR ACFEQSKNVA CVIIEALAGN MGFVPADKKF MQDLRALCDE YNALLIIDEV 

       250        260        270        280        290        300 
MSGFRAGLKG AIGLYDVQAD LVTYGKVIGG GMPLAAFGGR ADIMDMLSPV GGVYQAGTLS 

       310        320        330        340        350        360 
GNPIAVSAGL ATLLQIKANP TLYEHLEVLA KRLIKGLKEA AQSYEIPLQV DCRGSMFGFF 

       370        380        390        400        410        420 
FNQKEVKNFD DAKCSDTAMF ARFHQKMLDK GVYFACSQFE TGFICSAMNE MIIDEVIMKA 

       430 
KAVFGEITHE IESRI 

« Hide

References

[1]"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. expand/collapse author list , Shen Z., Weber J., Frosch M., Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017125 Genomic DNA. Translation: AAP77561.1.
RefSeqNP_860495.1. NC_004917.1.

3D structure databases

ProteinModelPortalQ7VHK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235279.HH0964.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP77561; AAP77561; HH_0964.
GeneID1492653.
KEGGhhe:HH0964.
PATRIC20589388. VBIHelHep90276_0961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMAHYPSIDM.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycHHEP235279:GHUA-993-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_HELHP
AccessionPrimary (citable) accession number: Q7VHK3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 78 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