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A9GDD3 (GSA_SORC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:sce9167
OrganismSorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) [Complete proteome] [HAMAP]
Taxonomic identifier448385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeSorangium

Protein attributes

Sequence length437 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 – 437437Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000079936

Amino acid modifications

Modified residue2791N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9GDD3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 9DCA109BD9136A59

FASTA43745,491
        10         20         30         40         50         60 
MTNATSAPPA RADRAPASKA LFDRAAAVLP GGVNSPVRAF RAVGGDPLFI ARAQGARLFD 

        70         80         90        100        110        120 
ADGAEYIDYV GSWGPAILGH AHPAVIEAVR EAALGGLSFG APTELEVRFA EKIRELYPSI 

       130        140        150        160        170        180 
DMLRCVSSGT EATMSAIRVA RGFTRRDAII KFEGCYHGHA DHLLVKAGSG LATFGAPDSA 

       190        200        210        220        230        240 
GVPESIARTT LSLPYNDPAA LEAAFAARGG DIAAVILEPV VGNMGCVPPE PGFLALVIDL 

       250        260        270        280        290        300 
CRKHGALSIF DEVMTGCRLA RGGAQERFGL RPDLTTLGKI VGGGMPLAAY GGRADVMRVV 

       310        320        330        340        350        360 
SPLGPVYQAG TLSGNPLAVT AGLATLDRLT PALYERLEEL GASLEEGLRA AAEGAGAAAC 

       370        380        390        400        410        420 
VQRVGSMITL FFTKGPVRSW ADAATSDTKR FSAFHAAMLA RGIYWPPSQY EAAFLSGAHS 

       430 
EEDIERTIAA CREALAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM746676 Genomic DNA. Translation: CAN99340.1.
RefSeqYP_001619820.1. NC_010162.1.

3D structure databases

ProteinModelPortalA9GDD3.
SMRA9GDD3. Positions 15-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING448385.sce9167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAN99340; CAN99340; sce9167.
GeneID5813273.
KEGGscl:sce9167.
PATRIC23677615. VBISorCel80414_9994.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAFADSTQN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSCEL448385:GJ75-9498-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_SORC5
AccessionPrimary (citable) accession number: A9GDD3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 46 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