Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P46716 (GSA_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. 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
Synonyms:gsa
Ordered Locus Names:ML2414
ORF Names:B2168_C1_190
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [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_0000120424

Amino acid modifications

Modified residue2791N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46716 [UniParc].

Last modified November 1, 1995. 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
U00018 Genomic DNA. Translation: AAA17225.1.
AL583925 Genomic DNA. Translation: CAC31930.1.
PIRS72889.
RefSeqNP_302563.1. NC_002677.1.

3D structure databases

ProteinModelPortalP46716.
SMRP46716. Positions 17-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML2414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31930; CAC31930; CAC31930.
GeneID908589.
KEGGmle:ML2414.
PATRIC18059451. VBIMycLep78757_4640.

Organism-specific databases

LepromaML2414.
CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

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_MYCLE
AccessionPrimary (citable) accession number: P46716
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 102 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