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B4EUE1 (GSA_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:PMI0205
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length428 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121909

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4EUE1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 0E71B3454B8435C2

FASTA42845,838
        10         20         30         40         50         60 
MSKSETLYNL AQQVIPGGVN SPVRAFNGVG GTPLFIERAN GAYIYDADGR AYLDYVGSWG 

        70         80         90        100        110        120 
PMVLGHNHPA IRHAVTDAVQ KGLSFGAPTA AEVEMANLVT ELVPSMDMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRDKIIKFEG CYHGHADCLL VKAGSGALTM GQPNSPGVPA DFVKHTLTCT 

       190        200        210        220        230        240 
YNDLNSVRQA FENYPEEIAC IIVEPVAGNM NCVPPKADFL PGLRALCDEF GALLIIDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAYYDVDPDL TCLGKIIGGG MPVGAFGGHK EVMSQLAPIG PVYQAGTLSG 

       310        320        330        340        350        360 
NPIAMAAGLA CLQEVSQPGV HQTLDELTTM LADGLLEKAQ QAGIPMVVNH VGGMFGLFFT 

       370        380        390        400        410        420 
DAKEVTCYQD VMNCDVERFK QFFHLMLEKR IYLAPSAFEA GFMSIAHSKE DIQRTIDAAE 


YAFSKMKA 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR40595.1.
RefSeqYP_002149986.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4EUE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI0205.

Proteomic databases

PRIDEB4EUE1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR40595; CAR40595; PMI0205.
GeneID6801596.
KEGGpmr:PMI0205.
PATRIC20515073. VBIProMir120933_0198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-204-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_PROMH
AccessionPrimary (citable) accession number: B4EUE1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 44 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