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

A6LKX4 (GSA_THEM4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Tmel_0711
OrganismThermosipho melanesiensis (strain BI429 / DSM 12029) [Complete proteome] [HAMAP]
Taxonomic identifier391009 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length423 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 – 423423Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382388

Amino acid modifications

Modified residue2591N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LKX4 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 8EC1CB662A8BC36D

FASTA42346,595
        10         20         30         40         50         60 
MFEKAKEFMP GGVNSPVRAF KSVELDPIFV KSAKGSKIKD INNNEYIDYI QSWGALILGH 

        70         80         90        100        110        120 
SHEVVINAIN EQSQKGTSYG LCHPLEVEMA QILVENIPSI EMVRMVNSGT EAVMSAIRLA 

       130        140        150        160        170        180 
RAYTKRDFIV KFEGCYHGHS DSLLVKAGSG ALTFGTPNSE GVTKEFVSKT IVAKYNDVQN 

       190        200        210        220        230        240 
INEIFENFGD KIACVIVEPI AGNMGVVPPK PNFLLTLRKL TKKYNSILIF DEVITGFRVS 

       250        260        270        280        290        300 
QNGAQGLFNV IPDLTTLGKV IGGGLPVGAF GGKKEIMQLI SPQGPVYQAG TLSGNPLTLA 

       310        320        330        340        350        360 
AGVSTLKFIL NNKNFYKKLD ELAKTLEEGL LYALKDFNIK VNRVGSMISF FFNGSSVDTY 

       370        380        390        400        410        420 
EKVISSDVNM YKKLFKYFLS YGILLPPSPF ESLFISYAHT NEDIQQTIDI AMKFSKNLKE 


GKV 

« Hide

References

[1]"Complete sequence of Thermosipho melanesiensis BI429."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BI429 / DSM 12029.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000716 Genomic DNA. Translation: ABR30575.1.
RefSeqYP_001305960.1. NC_009616.1.

3D structure databases

ProteinModelPortalA6LKX4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391009.Tmel_0711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR30575; ABR30575; Tmel_0711.
GeneID5297751.
KEGGtme:Tmel_0711.
PATRIC23922627. VBITheMel19269_0741.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycTMEL391009:GHM1-757-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_THEM4
AccessionPrimary (citable) accession number: A6LKX4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 24, 2007
Last modified: May 14, 2014
This is version 54 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