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A3NCF3 (GSA_BURP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:BURPS668_3011
OrganismBurkholderia pseudomallei (strain 668) [Complete proteome] [HAMAP]
Taxonomic identifier320373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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.

Sequence caution

The sequence ABN84156.1 differs from that shown. Reason: Erroneous initiation.

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_0000382288

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3NCF3 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 4A06BFA5B7C64E60

FASTA42744,809
        10         20         30         40         50         60 
MSNNQTLFER AQRTIPGGVN SPVRAFRSVG GTPRFVARAQ GAYFWDADGK RYIDYIGSWG 

        70         80         90        100        110        120 
PMIVGHVHPD VLAAVQHVLA DGFSFGAPTE AEIEIAEEIC KLVPSIEQVR MVSSGTEATM 

       130        140        150        160        170        180 
SALRLARGFT GRSRIVKFEG CYHGHADSLL VKAGSGLLTF GNPTSAGVPA DVAKHTTVLE 

       190        200        210        220        230        240 
YNNVAALEEA FAAFGGEIAA VIVEPVAGNM NLVRGTPEFL NALRALTAKH GAVLIFDEVM 

       250        260        270        280        290        300 
CGFRVALGGA QQHYGITPDL TCLGKVIGGG MPAAAFGGRG DIMSHLAPLG GVYQAGTLSG 

       310        320        330        340        350        360 
NPVAVAAGLA TLRLIQAPGF HDALADKTRR LADSLAAEAR AAGVPFSADA IGGMFGLYFT 

       370        380        390        400        410        420 
EQVPASFADV TKSDIERFNR FFHLMLDAGV YFAPSAYEAG FVSSAHDDAT LDATLDAARR 


AFAALRA 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 668.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000570 Genomic DNA. Translation: ABN84156.1. Different initiation.
RefSeqYP_001060024.1. NC_009074.1.

3D structure databases

ProteinModelPortalA3NCF3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320373.BURPS668_3011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN84156; ABN84156; BURPS668_3011.
GeneID4884563.
KEGGbpd:BURPS668_3011.
PATRIC19251727. VBIBurPse82117_2798.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycBPSE320373:GJ9C-3004-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_BURP6
AccessionPrimary (citable) accession number: A3NCF3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 59 of the entry and version 2 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