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Q1AUK6 (GSA_RUBXD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:Rxyl_1975
OrganismRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]
Taxonomic identifier266117 [NCBI]
Taxonomic lineageBacteriaActinobacteriaRubrobacteridaeRubrobacteralesRubrobacterineaeRubrobacteraceaeRubrobacter

Protein attributes

Sequence length439 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 – 439439Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382364

Amino acid modifications

Modified residue2771N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1AUK6 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 5244F27883CAC828

FASTA43946,865
        10         20         30         40         50         60 
MSGLQEARLR LARDRSARLM ERAVRRMPGG VNSPVRAFRS VGGDPLFMER GEGPRIFDAD 

        70         80         90        100        110        120 
GNAYIDYVMS YGPLLLGHAP PEVVGAVERA ARRGTTFGAP TRLEVELAEL VCEAVPSVEV 

       130        140        150        160        170        180 
VRMVNSGTEA TMSAVRLARG YTGREKILKF DGNYHGHGDA LLVSAGSGVA TLGLPDSPGV 

       190        200        210        220        230        240 
TPGAARDTAV LPYNDLEAVR ELFEERGEEF AAVILEPVAG NMGCIPPEEG FLEGLREITA 

       250        260        270        280        290        300 
ACGALLIFDE VMTGFRVSRG GAQERYGVVP DLTCLGKVIG GGLPVGAYGG RREIMERVAP 

       310        320        330        340        350        360 
AGPVYQAGTL SGNPLAMSAG LATLRRTGEP GFYERLEELG ARWERGMREA ASGSAVPVTV 

       370        380        390        400        410        420 
NRVGSMVSLF FASGPVRDFA SAAASDAELF KDFFWHMLSR GVYLAPSQYE AGFISLAHSE 

       430 
EEIDRTVEAA AEWFAGRRA 

« Hide

References

[1]"Complete sequence of Rubrobacter xylanophilus DSM 9941."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9941 / NBRC 16129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000386 Genomic DNA. Translation: ABG04922.1.
RefSeqYP_644734.1. NC_008148.1.

3D structure databases

ProteinModelPortalQ1AUK6.
SMRQ1AUK6. Positions 12-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266117.Rxyl_1975.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG04922; ABG04922; Rxyl_1975.
GeneID4115728.
KEGGrxy:Rxyl_1975.
PATRIC23370754. VBIRubXyl52678_1967.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycRXYL266117:GH8O-2010-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_RUBXD
AccessionPrimary (citable) accession number: Q1AUK6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 64 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