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A0QLG2 (GSA_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:MAV_4621
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length445 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 – 445445Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300924

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QLG2 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 67960C4069E62DDD

FASTA44545,471
        10         20         30         40         50         60 
MGSSDQATAH ARAQAASARL FDDACAVIPG GVNSPVRAFT AVGGTPPFIT AARGCRLTDA 

        70         80         90        100        110        120 
DGNHYVDLVC SWGPMILGHA HPAVVEAVAK AAASGLSFGA PTPAESELAA EMIARVAPVE 

       130        140        150        160        170        180 
RIRLVNSGTE ATMSAVRLAR GFTGRAKIVK FSGCYHGHVD ALLADAGSGV ATLGLPSSPG 

       190        200        210        220        230        240 
VTGATAADTI VLPYNDIDAV RQAFAEFGDQ IAAVITEASP GNMGVVPPAP GFNAALRALT 

       250        260        270        280        290        300 
AEHGALLIVD EVMTGFRVSR SGWYGIDPVD ADLFTFGKVM SGGLPAAAFG GRAEVMERLA 

       310        320        330        340        350        360 
PLGPVYQAGT LSGNPVAVAA GLATLRHADA AAYAALDANA DRLARLLSDA LTNAGVPHQI 

       370        380        390        400        410        420 
PRAGNMLSVF FTDTPVTDFA SARATQTWRY PPFFHALLDA GVYPPCSAFE TWFVSTALDD 

       430        440 
DAFDRIAAAL PAAARAAAGA DEGNS 

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000479 Genomic DNA. Translation: ABK67932.1.
RefSeqYP_883750.1. NC_008595.1.

3D structure databases

ProteinModelPortalA0QLG2.
SMRA0QLG2. Positions 15-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243243.MAV_4621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK67932; ABK67932; MAV_4621.
GeneID4525711.
KEGGmav:MAV_4621.
PATRIC17990936. VBIMycAvi38287_4537.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAADIAHEN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycMAVI243243:GH3Y-4621-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_MYCA1
AccessionPrimary (citable) accession number: A0QLG2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 52 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