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A4VQY0 (GSA_PSEU5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:PST_3758
OrganismPseudomonas stutzeri (strain A1501) [Complete proteome] [HAMAP]
Taxonomic identifier379731 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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_0000300938

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4VQY0 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: C8160122C27C14B2

FASTA42745,340
        10         20         30         40         50         60 
MSRSETLFAS AQTHIPGGVN SPVRAFRSVG GTPLFLKHAE GAYVIDEDDK RYVDYVGSWG 

        70         80         90        100        110        120 
PMILGHSHPQ VLDAVRRQLE HGLSYGAPTA METEMAELVC RLVPSMEMVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRDAIIKFEG CYHGHSDSLL VKAGSGALTQ GVPSSAGVPA DFAKHTLTLA 

       190        200        210        220        230        240 
YNDLDEVEAT LKEKGEQVAC IIVEPVAGNM NCVPPAPGFL EGLRRLCDAH GVVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAYYGVTPDL STFGKIIGGG MPVGCFGGKR AIMERIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGLT TLELISRPGF HDELGAYTSR MLQGLQDRAD AAGIPFVTTQ VGGMFGLYFS 

       370        380        390        400        410        420 
GADDIVTFAD VMASDADRFK RFFHLMLEGG VYLAPSAFEA GFTSIAHGDK ELAITLDAAE 


RAFAKLK 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y. expand/collapse author list , Elmerich C., Lin M., Jin Q.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000304 Genomic DNA. Translation: ABP81381.1.
RefSeqYP_001174223.1. NC_009434.1.

3D structure databases

ProteinModelPortalA4VQY0.
SMRA4VQY0. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379731.PST_3758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP81381; ABP81381; PST_3758.
GeneID5096719.
KEGGpsa:PST_3758.
PATRIC19968014. VBIPseStu31643_3736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPSTU379731:GJER-3753-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_PSEU5
AccessionPrimary (citable) accession number: A4VQY0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 48 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