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B2GL27 (GSA_KOCRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:KRH_08560
OrganismKocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201) [Complete proteome] [HAMAP]
Taxonomic identifier378753 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeKocuria

Protein attributes

Sequence length439 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 – 439439Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121899

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GL27 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 9D0E89A826ADDC97

FASTA43945,950
        10         20         30         40         50         60 
MSVSQELFDR ARRVMPGGVN SPVRAFNSVG GTPPFIAAAK GPYLTDVDGR EYVDLVCSWG 

        70         80         90        100        110        120 
PALIGHAHPV VTEAVHEAVE RGLGFGATTR GETELAELVV DRVAPLEEIR MVSTGTEATM 

       130        140        150        160        170        180 
TALRLARGYT GRDLVVKFAG CYHGHVDSLL SEAGSGLATL ALPGSAGVTE ATAAQTLVLP 

       190        200        210        220        230        240 
YNDVAALEAA FAEHPGRIAA VITEAAPCNM GVVTPQDGFN AAIRRITQAD GALMILDEVL 

       250        260        270        280        290        300 
TGFRVHEAGY WGLSNAAGES WAPDLFTFGK VIGGGLPTAA LGGRREVMEY LAPTGPVYQA 

       310        320        330        340        350        360 
GTLSGNPVAM AAGLATLKCA DAVAYQTIDR RSEQLRAGLR EALDAAGVDY SIQEVGSLFS 

       370        380        390        400        410        420 
LAFGTRSTGV HDYADAKGQE AFRYTPFFHA MLDAGVYLPP SVFEAWFLSA AHDDSAMDRI 

       430 
LSALPAAARA AAEAQPPQP 

« Hide

References

[1]"Complete genome sequence of the soil actinomycete Kocuria rhizophila."
Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
J. Bacteriol. 190:4139-4146(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9341 / DSM 348 / NBRC 103217 / DC2201.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009152 Genomic DNA. Translation: BAG29203.1.
RefSeqYP_001854709.1. NC_010617.1.

3D structure databases

ProteinModelPortalB2GL27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING378753.KRH_08560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG29203; BAG29203; KRH_08560.
GeneID6239487.
KEGGkrh:KRH_08560.
PATRIC22181926. VBIKocRhi5258_0832.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycKRHI378753:GJ8F-872-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.
ProtoNetSearch...

Entry information

Entry nameGSA_KOCRD
AccessionPrimary (citable) accession number: B2GL27
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 45 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