Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q48DP1 (GSA_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:PSPPH_4384
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243605

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48DP1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 4C2A41E807AFDFEE

FASTA42745,349
        10         20         30         40         50         60 
MSRSETLFAN AQKHIPGGVN SPVRAFKSVG GTPLFFKHAA GAYVTDEDDK RYVDYVGSWG 

        70         80         90        100        110        120 
PMILGHSHPE VLDAVRSQLE HGLSYGAPTA METEMADLVC ALVPSMEMVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGFT GRDSIIKFEG CYHGHSDSLL VKAGSGALTL GVPSSPGVPA AFAKHTLTVP 

       190        200        210        220        230        240 
FNNLDAVRDL LAEVGQEVAC IIVEPVAGNM NCVPPAPGYL QGLRDLCDEH GVVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAYYGVTPDL STFGKIIGGG MPVGCFGGKR EIMSHIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGLT TLRLISRPGF HDELSDYTRR LLEGLQQRAD AAGIAFVTTQ AGGMFGLYFS 

       370        380        390        400        410        420 
EAREIVTFED VMTSDAERFK RFFHLMLEGG VYLAPSAFEA GFTSIAHGDA ELKLTLDAAE 


KAFAALK 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ34622.1.
RefSeqYP_276500.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48DP1.
SMRQ48DP1. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_4384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ34622; AAZ34622; PSPPH_4384.
GeneID3557180.
KEGGpsp:PSPPH_4384.
PATRIC19978257. VBIPseSyr78478_4585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-4388-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_PSE14
AccessionPrimary (citable) accession number: Q48DP1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 66 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