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O74038 (GSA2_CENSY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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:gsaT
Ordered Locus Names:CENSYa_1168
OrganismCenarchaeum symbiosum (strain A) [Reference proteome] [HAMAP]
Taxonomic identifier414004 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaCenarchaealesCenarchaeaceaeCenarchaeum

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.

Subcellular location

Cytoplasm Potential.

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
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-EC

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 – 434434Glutamate-1-semialdehyde 2,1-aminomutase 2
PRO_0000120478

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O74038 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D1ED70D39A25CA50

FASTA43446,714
        10         20         30         40         50         60 
MDLEREYRAK TGGSARIFAR SKKYHVGGVS HNIRFYEPYP FVTRSASGKH LVDVDGNKYV 

        70         80         90        100        110        120 
DYWMGHWSLI LGHAPAPVRS AVEGQLRRGW IHGTVNEQTM NLSEIIRGAV SVAEKTRYVT 

       130        140        150        160        170        180 
SGTEAVMYAA RLARAHTGRK IIAKADGGWH GYASGLLKSV NWPYDVPESG GLVDEEHSIS 

       190        200        210        220        230        240 
IPYNDLEGSL DVLGRAGDDL ACVIIEPLLG GGGCIPADED YLRGIQEFVH SRGALLVLDE 

       250        260        270        280        290        300 
IVTGFRFRFG CAYAAAGLDP DIVALGKIVG GGFPIGVICG KDEVMEISNT ISHAKSDRAY 

       310        320        330        340        350        360 
IGGGTFSANP ATMTAGAAAL GELKKRKGTI YPRINSMGDD ARDKLSKIFG NRVSVTGRGS 

       370        380        390        400        410        420 
LFMTHFVQDG AGRVSNAADA AACDVELLHR YHLDMITRDG IFFLPGKLGA ISAAHSKADL 

       430 
KTMYSASERF AEGL 

« Hide

References

« Hide 'large scale' references
[1]"Genomic analysis reveals chromosomal variation in natural populations of the uncultured psychrophilic archaeon Cenarchaeum symbiosum."
Schleper C., Delong E.F., Preston C.M., Feldman R.A., Wu K.-Y., Swanson R.V.
J. Bacteriol. 180:5003-5009(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A.
[2]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083071 Genomic DNA. Translation: AAC62681.1.
DP000238 Genomic DNA. Translation: ABK77793.1.
RefSeqYP_876097.1. NC_014820.1.

3D structure databases

ProteinModelPortalO74038.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK77793; ABK77793; CENSYa_1168.
GeneID6371348.
KEGGcsy:CENSYa_1168.

Phylogenomic databases

HOGENOMHOG000020210.
KOK01845.
OMAEVITFRN.

Enzyme and pathway databases

UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR005814. 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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA2_CENSY
AccessionPrimary (citable) accession number: O74038
Secondary accession number(s): A0RWS6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 84 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