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Q7UPM9 (GSA_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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:RB6831
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

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
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 – 439439Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000226305

Amino acid modifications

Modified residue2791N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UPM9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 52F7D89E87373ADD

FASTA43945,935
        10         20         30         40         50         60 
MNSPANSSAA RPAAGPKSVA AFQRASALMP GGVNSPARAF GAVGGTPLFI ERAEGPYLYD 

        70         80         90        100        110        120 
IDGNRYIDYI GSWGPMILGH AHPEVINAIT QAAAKGTSYG APTEAESRLA EQIIEAVPSI 

       130        140        150        160        170        180 
EKVRLVNSGT EATMSALRVA RGATGRKKVI KFAGNYHGHV DSLLVAAGSA AATLGAPDSP 

       190        200        210        220        230        240 
GVTPGAAEDT LVLSYNDVSG LQNAFAQHGD DIAALILEPV VGNMGCVLPT MEFLNAARDL 

       250        260        270        280        290        300 
TTKHGSILIF DEVMTGFRVA YGGAQERFGV TPDMTTLGKI VGGGMPLGAY GGRADIMNQV 

       310        320        330        340        350        360 
LPAGKVFQAG TLSGNPVAVA AGSATLRLLK ENPPYEQLER LADRLADGLD RAATSAGMAH 

       370        380        390        400        410        420 
TVAKAGAMLT LFFNPEPVDC WAVADRCDRE AFGRYFWGLI DEGIYMPCSQ FEALFFSQQH 

       430 
TEAMIDETIA AAEKVLKSL 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294144 Genomic DNA. Translation: CAD75032.1.
RefSeqNP_867486.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UPM9.
SMRQ7UPM9. Positions 15-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB6831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD75032; CAD75032; RB6831.
GeneID1790380.
KEGGrba:RB6831.
PATRIC23248081. VBIRhoBal59814_3315.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBCLSK2759148.

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_RHOBA
AccessionPrimary (citable) accession number: Q7UPM9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 79 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