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C1DUY4 (GSA_SULAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:SULAZ_0948
OrganismSulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825) [Complete proteome] [HAMAP]
Taxonomic identifier204536 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaeSulfurihydrogenibium

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382384

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1DUY4 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 7A80879D7DD1AD31

FASTA42746,798
        10         20         30         40         50         60 
MNILKSKELF KEAQNYLVGG VNSPVRAFKA VGTDPIFIQR GKGSRIWDVD GNEYIDYVLS 

        70         80         90        100        110        120 
WGPLILGHAH DQVVNAIKQV ANYGTSFGAP TELEIEMAKA VVDAVKSVEM VRFVNSGTEA 

       130        140        150        160        170        180 
TMSAIRLARG YTKRKKIVKF DGCYHGHGDS LLVSAGSGVA TLGIPGTPGI PEELANLTIV 

       190        200        210        220        230        240 
LPYNDIEAVE EAFKRYGEDI ACVIIEPVAG NMGVVAPSKE YHQRLRDITR KYGALLIFDE 

       250        260        270        280        290        300 
VMTGFRLAYG GAQELYGIDP DLTTFGKVIG GGLPVGAYGG KREIMEYVAP VGPVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMAAG LRQLQLLKEL NPYRELDEKG RFLEEGFKQI AQEFSAAIQV NRVGSMITVF 

       370        380        390        400        410        420 
FTDIPVKDFA TAKTSDTNKF AKFFRCMLEK GIYLPASQFE AFFLSTAHSQ KDLEETLEKA 


RECFKIL 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Az-Fu1 / DSM 15241 / OCM 825.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001229 Genomic DNA. Translation: ACN98435.1.
RefSeqYP_002728921.1. NC_012438.1.

3D structure databases

ProteinModelPortalC1DUY4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204536.SULAZ_0948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN98435; ACN98435; SULAZ_0948.
GeneID7672681.
KEGGsaf:SULAZ_0948.
PATRIC23763024. VBISulAzo123226_0915.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSAZO204536:GHRE-947-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_SULAA
AccessionPrimary (citable) accession number: C1DUY4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 39 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