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Q0KDN9 (GSA_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:H16_A0734
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

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_0000300940

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0KDN9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: EA482CB26F350CB1

FASTA43045,452
        10         20         30         40         50         60 
MSRNQQLFDR AQQTIPGGVN SPVRAFRSVG GTPRFITRAE GAYMWDADGQ RYIDYIGSWG 

        70         80         90        100        110        120 
PMIVGHAHPE VVRAVQETAA HSFSFGAPTE AEITMAEEIC KLVPSIEQVR LVSSGTEATM 

       130        140        150        160        170        180 
SALRLARGFT GRDLIIKFEG CYHGHADSLL VKAGSGLLTF ADTTQNAPSS AGVPADVTRH 

       190        200        210        220        230        240 
TMVLEYNNVE QLEQAFARHA GEIAAVIVEP VAGNMNLVRA SDAFLKAMRE LCTRDGAVLI 

       250        260        270        280        290        300 
LDEVMTGFRV ALGGAQAHYG IRPDLTCLGK VIGGGMPAAA FGGRRDIMAR LAPLGGVYQA 

       310        320        330        340        350        360 
GTLSGNPLAV AAGLATLKLI QAPGFYDRLA SQTRKLADGL AEAAKAAGVP FAADAIGGMF 

       370        380        390        400        410        420 
GIYFREGVPG SFAEVTRSDT ARFNRFFHAM LDHGVYLAPS AFEAGFVSAQ HDDAILAATL 

       430 
EAARKAFAAG 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260479 Genomic DNA. Translation: CAJ91882.1.
RefSeqYP_725250.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0KDN9.
SMRQ0KDN9. Positions 3-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A0734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ91882; CAJ91882; H16_A0734.
GeneID4247050.
KEGGreh:H16_A0734.
PATRIC35230873. VBIRalEut6770_1105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAAIAGHAN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-733-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_CUPNH
AccessionPrimary (citable) accession number: Q0KDN9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 55 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