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A0LIP3 (GSA_SYNFM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Sfum_1608
OrganismSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB) [Complete proteome] [HAMAP]
Taxonomic identifier335543 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter

Protein attributes

Sequence length433 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 – 433433Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300954

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LIP3 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 072959F28932CE54

FASTA43346,361
        10         20         30         40         50         60 
MTRDRSNLLY EDAGRFIPGG VNSPVRSGRA VGTNPIFIRE AKGCYLWDED GNRYVDFVAS 

        70         80         90        100        110        120 
WGPLIVGHAH PAVVEAVRAA VEKGTSYGIP TEIEVRMARK VVEMVPSIEM VRMVNSGTEA 

       130        140        150        160        170        180 
TMSAIRLARG YTGRPGIIKF NGCYHGHGDC LLVKAGSGLA TFGIPGSPGV PEEVVRHTIP 

       190        200        210        220        230        240 
LSYNDLDEVE SVMERDGDRI AAIILEPVAA NMGLVLPRPG FLEGLRKLCD KHGALLIFDE 

       250        260        270        280        290        300 
VITGFRLARG GAQEFFGVTP DLTCLGKIIG GGLPVGAYGG RRDIMMKMAP VGNVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMAAG LATLDLLCED GVYESLEEKT NHLVDGLNEA AGAAGVPVFT SRIASLGCGF 

       370        380        390        400        410        420 
FTSEPVFDFA SALASNTDAY AVFFREMLNR GVYFAPAQFE AFFLSMAHES KDLDFTIEAA 

       430 
GNAFVRVKEL CAF 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000478 Genomic DNA. Translation: ABK17295.1.
RefSeqYP_845730.1. NC_008554.1.

3D structure databases

ProteinModelPortalA0LIP3.
SMRA0LIP3. Positions 1-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335543.Sfum_1608.

Proteomic databases

PRIDEA0LIP3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK17295; ABK17295; Sfum_1608.
GeneID4460108.
KEGGsfu:Sfum_1608.
PATRIC23848611. VBISynFum78438_1879.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAAKHTIVL.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSFUM335543:GH6P-1639-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_SYNFM
AccessionPrimary (citable) accession number: A0LIP3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 12, 2006
Last modified: May 14, 2014
This is version 54 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