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B2I6C2 (GSA_XYLF2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:XfasM23_1419
OrganismXylella fastidiosa (strain M23) [Complete proteome] [HAMAP]
Taxonomic identifier405441 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

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.

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 – 444444Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121931

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2I6C2 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 26BA479DAA49C8A9

FASTA44447,175
        10         20         30         40         50         60 
MNHSRSHALF VQAQTRIPGG VNSPVRAFRS VGGEPFFVAR ADGPYLFDVD GHRYIDYVGS 

        70         80         90        100        110        120 
WGPMIVGHNH PAVREAVQVA ISNGLSYGAP CAAEVTMAET IARLVPSCEM VRMVNSGTEA 

       130        140        150        160        170        180 
TLSAIRLARG ATGRNYIVKF EGCYHGHGDS FLVKGGSGML TLGIPSSPGV PAELSKLTIT 

       190        200        210        220        230        240 
LTYNDFDAAT ALFEEMGHHI AAVIVEPVIG NANCIPPQPG YLQHLRTLCT QYAVLLIFDE 

       250        260        270        280        290        300 
VMTGFRVALG GAQALYGVTP DLTTFGKIIG GGMPVGAYGG RRDLMQHIAP TGPIYQAGTL 

       310        320        330        340        350        360 
SGNPVAMAAG LAMLELIQAP DFYTHLSNAA AALCTGLQQA ASQAGIAMTT QQIGGMFGLF 

       370        380        390        400        410        420 
FTDQQVETYA QATACNTDRF NRFFHAMLQR GVFFAPSAYE AGFISSAHSP NIIETTLEAA 

       430        440 
RTAFQTIANE AAILSKSETP IKMR 

« Hide

References

[1]"Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001011 Genomic DNA. Translation: ACB92832.1.
RefSeqYP_001830106.1. NC_010577.1.

3D structure databases

ProteinModelPortalB2I6C2.
SMRB2I6C2. Positions 1-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405441.XfasM23_1419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB92832; ACB92832; XfasM23_1419.
GeneID6202331.
KEGGxfn:XfasM23_1419.
PATRIC24145155. VBIXylFas85937_1746.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycXFAS405441:GJJI-1454-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_XYLF2
AccessionPrimary (citable) accession number: B2I6C2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 45 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