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

Q1MPW7 (GSA_LAWIP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:LI0906
OrganismLawsonia intracellularis (strain PHE/MN1-00) [Complete proteome] [HAMAP]
Taxonomic identifier363253 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeLawsonia

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300921

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MPW7 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 148318A952B9F98A

FASTA43046,290
        10         20         30         40         50         60 
MQEESSKELY SKAVKLIPGG VNSPVRACRN VGCEPVFIES AKGAYLTTVD GQELLDFVLS 

        70         80         90        100        110        120 
WGAIILGHTN STVTNAIKKA ASNGTTFGAP CKAEVLLAKE IIDAFPGMDM IRMVSSGTEA 

       130        140        150        160        170        180 
TMSALRLARG VTGRNKVLKF IGCYHGHADP FLASAGSGVA TLSIPGTPGV PEVTVRDTLL 

       190        200        210        220        230        240 
APYNDLSTVK DLFVMYGKDL AAVFVEPIAA NMGLIPPKEG FLKGLRALCD AHGTLLIMDE 

       250        260        270        280        290        300 
VITGFRVAYG GAQTRFDITP DLTTLGKIIG GGLPIGAYGG KAKYMEHIAP LGEIYQAGTL 

       310        320        330        340        350        360 
SGNPLVMTAG FETLQLLKDI NYTILEKQVA TFANELEVIL KDKGVPVQVS NFASMFTVFF 

       370        380        390        400        410        420 
TNNELKSFDD VKTTNTQLYS ILFRSMQKNN IFLVPSPFET NMVSFAHKEK EFEKALIAAK 

       430 
KIMFNITDVN 

« Hide

References

[1]"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHE/MN1-00.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180252 Genomic DNA. Translation: CAJ54960.1.
RefSeqYP_595281.1. NC_008011.1.

3D structure databases

ProteinModelPortalQ1MPW7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING363253.LI0906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4060263.
KEGGlip:LI0906.
PATRIC22305323. VBILawInt40445_0982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACGHANER.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLINT363253:GH6E-939-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_LAWIP
AccessionPrimary (citable) accession number: Q1MPW7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 53 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