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Q9KEB0 (GSA1_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. 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 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Synonyms:gsaB
Ordered Locus Names:BH0943
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length437 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 – 437437Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000120394

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KEB0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F2035E49347BE0A7

FASTA43747,080
        10         20         30         40         50         60 
MNRSRSESLF QKAQSLIVGG VNSPSRSFKA VGGGAPVFME KAKGAYFWDV DGNQYIDYLA 

        70         80         90        100        110        120 
AYGPIITGHA HPHITNAIQR AAENGVLYGT PTKLENQFAS MLQQAIPSLE KVRFVNSGTE 

       130        140        150        160        170        180 
AVMTTIRVAR AYTGRDKIIK FAGCYHGHSD LVLVAAGSGP STLGTPDSAG VTKNIAEEVI 

       190        200        210        220        230        240 
TVPFNQLDSL KEALDHWGEE VAAVLVEPIV GNFGIVEPHE GFLEGVNELA HNAGALVIYD 

       250        260        270        280        290        300 
EVITAFRFMY EGAQNYVGVE PDMTALGKII GGGLPIGAYG GRIDIMEKVA PLGPAYQAGT 

       310        320        330        340        350        360 
MAGNPASMSA GIACLEVLQE EGLYDELDRK GAILEKGIKA HAEAHGITIS INRLKGALTV 

       370        380        390        400        410        420 
YFTDETVTCY EQAERSDGEK FSLFFKEMLN QGINLAPSKY EAWFLTIAHT DEDIEKTLQA 

       430 
VDHAFSVMAA KGYHLKR 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04662.1.
PIRG83767.
RefSeqNP_241809.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KEB0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH0943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB04662; BAB04662; BAB04662.
GeneID893889.
KEGGbha:BH0943.
PATRIC18938906. VBIBacHal18977_0991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAITINRLK.
OrthoDBEOG6QVRHN.
ProtClustDBPRK12389.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-1001-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 nameGSA1_BACHD
AccessionPrimary (citable) accession number: Q9KEB0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 97 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