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A5W9H0 (GSA_PSEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Pput_4660
OrganismPseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]
Taxonomic identifier351746 [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_1000059998

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5W9H0 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 963714366FD016B6

FASTA42745,124
        10         20         30         40         50         60 
MSRSEALFAQ AQKHIPGGVN SPVRAFKSVG GTPLFFKHAE GAYVVDEDDK RYVDYVGSWG 

        70         80         90        100        110        120 
PMILGHGHPD VLDSVRKQLE HGLSYGAPTA METEMADLVC SIVPSMEMVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRDAIIKFEG CYHGHSDSLL VKAGSGLLTQ GVPSSAGVPA DFAKHTLTLP 

       190        200        210        220        230        240 
FNDIAAVEKT LAEVGQTVAC IIVEPVAGNM NCVPPAPGFL EGLREQCDKH GVVLIFDEVM 

       250        260        270        280        290        300 
TGFRVSLGGA QGHYGITPDL STFGKIVGGG MPVGCFGGKR EIMGCIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGLT TLKLISRPGF HAELTDYTSR MLDGLQQRAD AAGVPFVTTQ AGAMFGLYFS 

       370        380        390        400        410        420 
GADDIVTFED VMASDAERFK RFFHLMLDGG VYLAPSAFEA GFTSIAHGDK ELQITLDAAE 


KAFAALK 

« Hide

References

[1]"Complete sequence of Pseudomonas putida F1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F1 / ATCC 700007.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000712 Genomic DNA. Translation: ABQ80780.1.
RefSeqYP_001269964.1. NC_009512.1.

3D structure databases

ProteinModelPortalA5W9H0.
SMRA5W9H0. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351746.Pput_4660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ80780; ABQ80780; Pput_4660.
GeneID5190519.
KEGGppf:Pput_4660.
PATRIC19925562. VBIPsePut56420_4723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPPUT351746:GI26-4751-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_PSEP1
AccessionPrimary (citable) accession number: A5W9H0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 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