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Q9RWW0 (GSA_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. 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:DR_0555
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length444 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.

Sequence caution

The sequence AAF10132.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference 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 – 444444Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120407

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RWW0 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 344BFE4E3107A8C8

FASTA44446,305
        10         20         30         40         50         60 
MTLSETHPTA RSEALFVRAR AVTPGGVNSP VRAFRSVGGV PRFIASAQGA YLTDADGARY 

        70         80         90        100        110        120 
LDYIGSWGPM ILGHNHPAVR DAVAQALASG TSFGAPNERE VELAELIVEL TGAERVRFVS 

       130        140        150        160        170        180 
SGTEATMSAL RLARGYTGRK FIVKFRGNYH GHADGLLVEA GSGLLTNAEG DLGAAAPSSA 

       190        200        210        220        230        240 
GVPEEYAGLT LVLDYNDPEA LDALMAQRGD EIAAVIFEPV VGNAGVLIPT SDFLAALHRV 

       250        260        270        280        290        300 
RDFGAVLIAD EVMTGFRLSL NGATGLLSLD PDLRCWGKIV GGGLPVGAYG GRADIMDFVS 

       310        320        330        340        350        360 
PQGPVYQAGT LSGNPLAMAA GIATLRELKA NPGLYRQLDE YAARLAAGLR GAAERAGVAV 

       370        380        390        400        410        420 
SINHIGSMLT VFFQDAPDGS VRDYAAAARS DTAAFAAWFQ GLLARGIYWA PSQFESIFIS 

       430        440 
AAHGEPELAA TLEAAAQAFE GVKP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF10132.1. Different initiation.
PIRE75505.
RefSeqNP_294278.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RWW0.
SMRQ9RWW0. Positions 12-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_0555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF10132; AAF10132; DR_0555.
GeneID1799707.
KEGGdra:DR_0555.
PATRIC21628634. VBIDeiRad64572_0730.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycDRAD243230:GH46-569-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_DEIRA
AccessionPrimary (citable) accession number: Q9RWW0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 101 of the entry and version 2 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