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Q92AX5 (GSA2_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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 2

Short name=GSA 2
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name=GSA-AT 2
Gene names
Name:hemL2
Synonyms:gsaB
Ordered Locus Names:lin1793
OrganismListeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]
Taxonomic identifier272626 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length432 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000120420

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92AX5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: ABDBB12358D71A80

FASTA43246,009
        10         20         30         40         50         60 
MDHSMSKKLH DEALLHIVGG VNSPSRSNKG VGGGIPVTME RANGAYFYDV DGNKYIDYLA 

        70         80         90        100        110        120 
AFGPIITGHA HPHITEAITK AAQNGVLYGT PTKHEITFAK MLKEAIPSLE KVRFTNSGTE 

       130        140        150        160        170        180 
AVMTTIRVAR AYTGRDKIIK FAGCYHGHFD LVLVEAGSGP STLGIPDSAG VTRSTAEEVI 

       190        200        210        220        230        240 
TVPFNDLTSF KEALAVWGDQ VAAVLVEPIV GNFGMVAPAE GFLEAVNELA HENGSLVIYD 

       250        260        270        280        290        300 
EVITAFRFMY GGAQNYLGVI PDLTAMGKII GGGLPIGAYG GRVDIMEKVA PLGPAYQAGT 

       310        320        330        340        350        360 
HAGNPASILS GIACLEVLQE EGLYDRFEKY GSMLKEGIEK AAIKHGIAVT VNQIVGALTV 

       370        380        390        400        410        420 
YFTDEPVTNY AEAGATNGDL FGRFFKGMLE EGINLAPSKY EAWFITSAHS EADILETIQA 

       430 
VDTVFGKLVQ GK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596170 Genomic DNA. Translation: CAC97024.1.
PIRAH1656.
RefSeqNP_471129.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ92AX5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272626.lin1793.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC97024; CAC97024; CAC97024.
GeneID1130465.
KEGGlin:lin1793.
PATRIC20300391. VBILisInn102668_1838.

Organism-specific databases

GenoListLIN1793.
CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAETRANGM.
OrthoDBEOG6QVRHN.

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 nameGSA2_LISIN
AccessionPrimary (citable) accession number: Q92AX5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 83 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