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B6J3H2 (GSA_COXB2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:CbuG_0257
OrganismCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP]
Taxonomic identifier434923 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length435 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 – 435435Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121873

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J3H2 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 5656419F51CEECD5

FASTA43546,401
        10         20         30         40         50         60 
MVDHSAALFN KAQNYMPGGV NSPVRAFGAV GGVPRFIKKA SGPYLIDVDE KKYIDYVGSW 

        70         80         90        100        110        120 
GPMILGHAHP AVIQAAQEAV QNGLSFGAPC ENEIKLAALI GEFMPSIEKV RMVNSGTEAT 

       130        140        150        160        170        180 
MSALRLARGV TGRSKIIKFE GCYHGHADCL LVNAGSGALT FGMPSSPGVP LGTVQDTLTA 

       190        200        210        220        230        240 
TFNDLDSVAA LFEKYSKDIA AIIVEPIAGN MNLIPAAPDF LTGLRELCNQ YGSLLIFDEV 

       250        260        270        280        290        300 
ITGFRVAKGG AQSLYNIRPD LTALGKIIGG GMPVGAYGGR REIMNQLSPE GPVYQAGTLS 

       310        320        330        340        350        360 
GNPVAMAAGL ATLKELTAEN FYSNLKEKTE RLVMGILSRA KAAKIPLTAN FSCGIFGLIF 

       370        380        390        400        410        420 
TSEGRVTRYA QAVNGNVEHF RSFFHKMLDN GVYLAPSAFE SGFISAAHTN KEVDKTLDII 

       430 
ENIFSVSETY LRISV 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuG_Q212.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001019 Genomic DNA. Translation: ACJ17698.1.
RefSeqYP_002302843.1. NC_011527.1.

3D structure databases

ProteinModelPortalB6J3H2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434923.CbuG_0257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ17698; ACJ17698; CbuG_0257.
GeneID7012673.
KEGGcbg:CbuG_0257.
PATRIC17911511. VBICoxBur10955_0247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCBUR434923:GC8S-257-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_COXB2
AccessionPrimary (citable) accession number: B6J3H2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 42 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