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B8ZT67 (GSA_MYCLB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:MLBr02414
OrganismMycobacterium leprae (strain Br4923) [Complete proteome] [HAMAP]
Taxonomic identifier561304 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length446 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 – 446446Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201027

Amino acid modifications

Modified residue2791N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8ZT67 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 1C684412C451FF6F

FASTA44645,790
        10         20         30         40         50         60 
MGSTDQATAP AGPAVSISAK LFEDACAVIP GGVNSPVRAF SAVGGTPLFI TEARGCWLTD 

        70         80         90        100        110        120 
ADGRRYVDLV CSWGPMILGH AHPAVVDAVA TVAASGLSFG APTPAETQLA AEIIGRMAPV 

       130        140        150        160        170        180 
ERIRLVNSGT EATMSAVRLA RGFTGRTKII KFSGCYHGHV DALLADAGSG VATLSLPSSP 

       190        200        210        220        230        240 
GVTGAAAADT IVLPYNDIEA VRQTFARLGD QIAAVITEAS PGNMGVVPPA PGYNAALRAI 

       250        260        270        280        290        300 
TAEHGALLII DEVMTGFRVS RSGWYGLDPV AADLFIFGKV MSGGMPAAAF GGRAEVMERL 

       310        320        330        340        350        360 
APLGPVYQAG TLSGNPVAMA AGLATLRAAA DAVYATLDRN ADRLVAMLSE ALTDAGVPHQ 

       370        380        390        400        410        420 
IPRAGNMFSV FFSEAPVTDF ASACNSQVWR YPAFFHALLD AGVYPPCSTF EAWFVSAALD 

       430        440 
DAAFGRIVDA LPGAAAAAVA ARHRES 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM211192 Genomic DNA. Translation: CAR72512.1.
RefSeqYP_002504193.1. NC_011896.1.

3D structure databases

ProteinModelPortalB8ZT67.
SMRB8ZT67. Positions 17-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561304.MLBr_02414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR72512; CAR72512; MLBr02414.
GeneID7324736.
KEGGmlb:MLBr_02414.
PATRIC18048921. VBIMycLep121698_4660.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycMLEP561304:GJP6-2467-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_MYCLB
AccessionPrimary (citable) accession number: B8ZT67
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 41 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