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

Q2FTK5 (GSA_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:Mhun_2560
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference 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 – 417417Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382409

Amino acid modifications

Modified residue2631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FTK5 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 87CE37FF3AF98598

FASTA41744,370
        10         20         30         40         50         60 
MSEKSREYYT IARDLMPGGV SSPVRAIQPY PFYTVRGSGS RIYTVDGTEL IDCCGAYGPL 

        70         80         90        100        110        120 
ILGHACKPVG DAISSALDDG WLYGTPTPAE IDLAQILIAD HPSIEMVRFV TTGSEATMAA 

       130        140        150        160        170        180 
IRLARGYTGK SDIIKTEGGF HGAHDGVLVQ AGSGCTTLGQ PDSAGVLSDI VRHTRQVPYN 

       190        200        210        220        230        240 
DTESLISLVD KSGDEIAAMI LEPVMGNIGP VLPKPGYLQE VRKITAEHDI LLIFDEVITG 

       250        260        270        280        290        300 
YRVGIGGAQK LFGVTPDITT LGKIIGGGLP LSAFGGKRKI MELIAPAGPV YQAGTFSGNP 

       310        320        330        340        350        360 
LSLAAGVAAL REIHARKGMY TLLDTATTVI GEACQGKGGS FVKLGSMFKF FFRSSVPENY 

       370        380        390        400        410 
AQAKESDTTK FRAFWEKMLE KGIFLPPSQF ETNFLSAAHS DSDVEYLSSA YASCLSA 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD42259.1.
RefSeqYP_503978.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FTK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_2560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD42259; ABD42259; Mhun_2560.
GeneID3922817.
KEGGmhu:Mhun_2560.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-2597-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_METHJ
AccessionPrimary (citable) accession number: Q2FTK5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 63 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