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Q6AHE8 (GSA_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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:Lxx01130
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length447 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 – 447447Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120416

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AHE8 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: C080E3476230A568

FASTA44745,819
        10         20         30         40         50         60 
MAAAAIGEAN LAQFGRAQRV IPGGVNSPVR AFRSVGGTPR FMVFANGPYI VDAEGREYVD 

        70         80         90        100        110        120 
LVASWGPAIL GHAHPAVVSA VQEAAARGLS FGASTPAETE LAEAVIARVP FVEKLRLVST 

       130        140        150        160        170        180 
GTEATMTAIR LARGFTGRPL LIKFAGHYHG HSDSLLAEAG SGLATLSLPG SAGVTEATAA 

       190        200        210        220        230        240 
QTLVLPYNDL GAVRAVFEAN GPDIAAVIAE AAAANMGVVP PDEGFNAALT DLAHEYGALL 

       250        260        270        280        290        300 
ILDEVLTGFR VSEAGFWGLD RGYTPDLVAF GKVIGGGMPL AAVGGRAELM DILAPAGPVY 

       310        320        330        340        350        360 
QAGTLSGNPV AVAAGLATLA HAGEAVYDRL DIVAGTLSAA VSDALTAEGV AHSVQRAGNL 

       370        380        390        400        410        420 
FSFVFGDVAA APRTFAEVQR QEAFRYRAFF HAMLDAGVSL PPSVFEAWFV TAAHDDAAVG 

       430        440 
RVLEALPAAA RAAASACPGR PLLFVRR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT88197.1.
RefSeqYP_061302.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6AHE8.
SMRQ6AHE8. Positions 11-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281090.Lxx01130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT88197; AAT88197; Lxx01130.
GeneID2940479.
KEGGlxx:Lxx01130.
PATRIC22333666. VBILeiXyl11655_0111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARFMVSGN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-103-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_LEIXX
AccessionPrimary (citable) accession number: Q6AHE8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 74 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