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Q13V40 (GSA_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Bxeno_A3511
ORF Names:Bxe_A0896
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300898

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q13V40 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: E6851D891918EF7D

FASTA42745,462
        10         20         30         40         50         60 
MSKNETLFER AQRTIPGGVN SPVRAFRSVG GTPRFIERAQ GAYFWDADGQ RYIDYIGSWG 

        70         80         90        100        110        120 
PMILGHVHPE VLEAVQRVLG NGFSFGAPTE SEVEIAEEIC KLVPSIEQVR MVSSGTEATM 

       130        140        150        160        170        180 
SALRLARGFT NRTRIVKFEG CYHGHADSLL VKAGSGLLTF GNPTSAGVPA DIAKHTTVLE 

       190        200        210        220        230        240 
YNNVAELEEA FKAFGNEIAS VIVEPVAGNM NLVRATPEFL QALRRLCSEY GSVLIFDEVM 

       250        260        270        280        290        300 
CGFRVALGGA QEVYGITPDL TCLGKVIGGG MPAAAFGGRR DIMAHLAPLG GVYQAGTLSG 

       310        320        330        340        350        360 
NPIAVAAGLK TLQLIQAPGF YDTLAARTTR LAQGLANVAR EARVPFAADS LGGMFGLYFT 

       370        380        390        400        410        420 
ESIPTSFAEV TQSDVPRFNA FFHKMLDAGV YFAPSAYEAG FVSIVHDDAI IDATIDAARG 


AFASLAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000270 Genomic DNA. Translation: ABE32049.1.
RefSeqYP_560101.1. NC_007951.1.

3D structure databases

ProteinModelPortalQ13V40.
SMRQ13V40. Positions 3-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266265.Bxe_A0896.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE32049; ABE32049; Bxe_A0896.
GeneID4002837.
KEGGbxe:Bxe_A0896.
PATRIC19332785. VBIBurXen52548_3689.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBXEN266265:GJII-3652-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_BURXL
AccessionPrimary (citable) accession number: Q13V40
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 54 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