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

B1YJU8 (GSA2_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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
Ordered Locus Names:Exig_2134
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length436 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 – 436436Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382314

Amino acid modifications

Modified residue2711N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YJU8 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 4EB5B02EF18C056D

FASTA43647,038
        10         20         30         40         50         60 
MSLTNQNSKS KAAFERALPL MPGGVNSPVR AYKSVGMTPI FAERAQGSRL YDIDGKEYID 

        70         80         90        100        110        120 
YVLSWGPMIL GHADPIVTAA IQEQATRGWS YGTPTEIESA MAEVVISRVP SVEVVRMVNS 

       130        140        150        160        170        180 
GTEATMAALR LARGYTGKTK ILKFEGCYHG HGDSLLIKAG SGVATLGLPD SPGVPAQIAS 

       190        200        210        220        230        240 
MTLTVPYNDM DAVRIAFEKH GDDIAGVIVE PAAGNMGFVP PQPGFLEGLR EITEQHGTLL 

       250        260        270        280        290        300 
IFDEVMTGFR VGFNCAQGHF GVTPDITCLG KVIGGGMPVG AYGGRRDIME QIAPQGPIYQ 

       310        320        330        340        350        360 
AGTLSGNPLA MAAGLATLTQ LKPEHYEEFD RKANRLSEGY LAAAAKYNIP LTTNRAGAMF 

       370        380        390        400        410        420 
GVFFTDQPVT NFEQAKSSNL DMFRSYYQKM AARGVFLPPS QFEGLFLSTV HTDDDIEQTL 

       430 
AAVELTFKEL QLEFNR 

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001022 Genomic DNA. Translation: ACB61586.1.
RefSeqYP_001814603.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YJU8.
SMRB1YJU8. Positions 39-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262543.Exig_2134.

Proteomic databases

PRIDEB1YJU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB61586; ACB61586; Exig_2134.
GeneID6173802.
KEGGesi:Exig_2134.
PATRIC32137892. VBIExiSib53410_2169.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycESIB262543:GHBP-2213-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 nameGSA2_EXIS2
AccessionPrimary (citable) accession number: B1YJU8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 49 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