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

Q12WM7 (GSA_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Mbur_1227
OrganismMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 – 422422Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382398

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12WM7 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 2ECCECF446F7FFD7

FASTA42245,657
        10         20         30         40         50         60 
MVTLDKSKDL FDKARKILPG GVSSPVRAIK PYPFYTESAN GCRIKDVDGN EYIDYCLAYG 

        70         80         90        100        110        120 
PNILGHANPV IKQAIIDQLD KGWLYGTPTG LEVTLGEKIA SLYPSIDMLR FVSTGTEATM 

       130        140        150        160        170        180 
SALRAARGFT CKNKFVKIEG GFHGAHDAVL VKAGSGATTH GKPDSLGIPE DFTKNTLQVA 

       190        200        210        220        230        240 
YNDIEAMTEV IESNQDDMAA VIMEPVLGNI GPILPEGDYL KEVRKVTEEN DVVLIFDEVI 

       250        260        270        280        290        300 
TGFRLAMGGA QEYFGVTPDM TTLGKIVGGG LPIGVFGGKR EILEMISPSG SVYQAGTFSG 

       310        320        330        340        350        360 
SPASVAAGIA AVDVLEKEKV HEKLEATGNM LRAGLNDIIA DKRLDFHVGG IASMFKVFFG 

       370        380        390        400        410        420 
DKPLNYQDVL KCDKEGYLQF FHDMLDSNVF LPPSQFETNF LSTAHTEADL ETTLEAYAVN 


LK 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE52149.1.
RefSeqYP_565899.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12WM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259564.Mbur_1227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE52149; ABE52149; Mbur_1227.
GeneID3998551.
KEGGmbu:Mbur_1227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycMBUR259564:GHBZ-1250-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_METBU
AccessionPrimary (citable) accession number: Q12WM7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 61 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