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Q7N845 (GSA_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:plu0902
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

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_0000120430

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N845 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 48B9A87C545C2386

FASTA42745,710
        10         20         30         40         50         60 
MSQSDILYSQ AKQLIPGGVN SPVRAFNGVG GTPLFIKHAD GAYLYDVDGK AYIDYVGSWG 

        70         80         90        100        110        120 
PMVLGHNHSA IRNAVIKAAE QGLSFGAPTA AEVEMAQLVT ELVPSMDMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT HRDKIIKFEG CYHGHADCLL VKAGSGALTI GQPNSPGVPV DFVKHTLTCT 

       190        200        210        220        230        240 
YNDLSSVREA FEQYPQEIAC IIVEPVAGNM NCVPPQPEFL PGLRALCDEF GALLIIDEVM 

       250        260        270        280        290        300 
TGFRVALSGA QSYYDVEPDI TCLGKIIGGG MPVGAFGGRY EVMEKLAPIG PVYQAGTLSG 

       310        320        330        340        350        360 
NPIAMAAGLA CLKEVSQPGV HQRLTELTDN LAAGLTKSAK AANIPLVVNH VGGMFGIFFT 

       370        380        390        400        410        420 
DAETVTCYQD VMNCDIERFK HFFHLMLDEG VYLAPSAFEA GFMSIAHTDE DIQRTVNAAA 


RCFAKLK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571861 Genomic DNA. Translation: CAE13197.1.
RefSeqNP_928238.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N845.
SMRQ7N845. Positions 3-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243265.plu0902.

Proteomic databases

PRIDEQ7N845.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE13197; CAE13197; plu0902.
GeneID2800865.
KEGGplu:plu0902.
PATRIC20505439. VBIPhoLum48522_0993.

Organism-specific databases

GenoListplu0902.
CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_PHOLL
AccessionPrimary (citable) accession number: Q7N845
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 75 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