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Q3K6C0 (GSA_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:Pfl01_4947
OrganismPseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]
Taxonomic identifier205922 [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_0000243604

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3K6C0 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E0E11C0D610FD8A7

FASTA42745,123
        10         20         30         40         50         60 
MSRSETLFAN AQKHIPGGVN SPVRAFKSVG GTPLFFKHAE GAYVTDEDDK RYVDYVGSWG 

        70         80         90        100        110        120 
PMILGHSHPD VLDAVRNQLQ HGLSYGAPTA METEMADLVC SLVPSLEMVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGFT GRDSIIKFEG CYHGHSDSLL VKAGSGALTQ GVPSSAGVPA AFAKHTLTLP 

       190        200        210        220        230        240 
FNDIDAVEKM LAEVGQDVAC IIVEPVAGNM NCVPPAPGFL EGLRSLCDKH GVVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAYYGVTPDL TTFGKIIGGG MPVGCFGGKR LIMERIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGLT TLRLISRPGF HAELTDYTTR LLDGLQQRAD AAGIPFVTTQ AGGMFGLYFS 

       370        380        390        400        410        420 
GADDIVTFED VMASDAALFG RFFHLMLEGG VYLAPSAFEA GFTSIAHGEA ELKLTLDAAE 


RAFAKLK 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000094 Genomic DNA. Translation: ABA76684.1.
RefSeqYP_350675.1. NC_007492.2.

3D structure databases

ProteinModelPortalQ3K6C0.
SMRQ3K6C0. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205922.Pfl01_4947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA76684; ABA76684; Pfl01_4947.
GeneID3714030.
KEGGpfo:Pfl01_4947.
PATRIC19892092. VBIPseFlu44242_4961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPFLU205922:GJBD-5026-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_PSEPF
AccessionPrimary (citable) accession number: Q3K6C0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 72 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