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A6Q9P9 (GSA_SULNB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:SUN_1254
OrganismSulfurovum sp. (strain NBC37-1) [Complete proteome] [HAMAP]
Taxonomic identifier387093 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaSulfurovum

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_1000060003

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6Q9P9 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 8ED3F48106CAEBC3

FASTA43045,655
        10         20         30         40         50         60 
MAYDKSIAAF EEAYKVIPGG VDSPVRAFSG VEGTPPFIER GEGAYLFDID GNRYIDYVQS 

        70         80         90        100        110        120 
WGPLIFGHTD ADIEASVIDS VKKGLSFGAP TTVETELAEE IVLMFESIDK VRFVSSGTEA 

       130        140        150        160        170        180 
VMSAIRLARG ATGRDNILKF TGCYHGHSDS LLVQAGSGLA TFGTPSSPGV PADLTKHTLL 

       190        200        210        220        230        240 
GTYNDIESVE KCFADSPEGI ACVIIEPIAG NMGLVPADET FLQQLRALCD AHGTLLIFDE 

       250        260        270        280        290        300 
VMSGFRASLK GAQGITTVKP DMVTLGKVIG AGMPVGAFGA GAETMAQLSP EGPVYQAGTL 

       310        320        330        340        350        360 
SGNPVAMAAG LTSLRKLKAN PAIYVELGNK AKKLVEGLKR AADSVNVPMV TDVRGSMFGF 

       370        380        390        400        410        420 
FFSDKPVKNF ADAMENDQKL FAKFHKGMLD RGIYLACSSF ETGFISTAIT DEMIDETVKA 

       430 
AYETLKEIKG 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBC37-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009179 Genomic DNA. Translation: BAF72208.1.
RefSeqYP_001358565.1. NC_009663.1.

3D structure databases

ProteinModelPortalA6Q9P9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387093.SUN_1254.

Proteomic databases

PRIDEA6Q9P9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF72208; BAF72208; SUN_1254.
GeneID5363366.
KEGGsun:SUN_1254.
PATRIC23775485. VBISulSp49917_1271.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSSP387093:GH25-1269-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_SULNB
AccessionPrimary (citable) accession number: A6Q9P9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 49 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