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A8LCD0 (GSA_FRASN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Franean1_6123
OrganismFrankia sp. (strain EAN1pec) [Complete proteome] [HAMAP]
Taxonomic identifier298653 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length449 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 – 449449Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121889

Amino acid modifications

Modified residue2751N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LCD0 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 365C8E44EBFE87F0

FASTA44945,740
        10         20         30         40         50         60 
MVVPSTAPAS DDLFRRAQRV VPGGVNSPVR AFRAVGGTPR FMTSGSGPRL VDADGRTYVD 

        70         80         90        100        110        120 
LVCSWGPMIL GHAHPDVVQA ITAAAARGTS FGTPTPGEVE LAELIVERVA PVEQVRLVNS 

       130        140        150        160        170        180 
GTEATMSAIR LARGFTGRPT IVKFAGCYHG HVDALLASAG SGVATLGLPD TPGVTGAATA 

       190        200        210        220        230        240 
DTIVLPYNDL ALVEATFAER GDTIAAVITE SVAANMGVVP PLPGFNAGLR RLCDAHGALL 

       250        260        270        280        290        300 
VFDEVMTGFR VSRTGWWGLE GAVEGWAPDL FTFGKVMGGG LPAAAFGGRA DVMARLAPAG 

       310        320        330        340        350        360 
PVYQAGTLSG NPLAVAAGLA TLRACTDEVY ATVDARAADV AGIVSTALNE QGVPHLLNSA 

       370        380        390        400        410        420 
GSLFSVFFTD ATAVIDYAGA KRQASERYAA FFHSMLDAGV YLPPSAFEAW FVSAAHDDEA 

       430        440 
VERIAAAAPA AARAAAAVGA PVAVGGGAV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000820 Genomic DNA. Translation: ABW15467.1.
RefSeqYP_001510373.1. NC_009921.1.

3D structure databases

ProteinModelPortalA8LCD0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298653.Franean1_6123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW15467; ABW15467; Franean1_6123.
GeneID5674444.
KEGGfre:Franean1_6123.
PATRIC21945787. VBIFraSp51419_6490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycFSP298653:GHPI-6154-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_FRASN
AccessionPrimary (citable) accession number: A8LCD0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 51 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