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Q2P6E4 (GSA_XANOM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:XOO1128
OrganismXanthomonas oryzae pv. oryzae (strain MAFF 311018) [Complete proteome] [HAMAP]
Taxonomic identifier342109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length429 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243646

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2P6E4 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: A152440E37ABBD20

FASTA42944,904
        10         20         30         40         50         60 
MNHSRSHALF AQAQTVLPGG VNSPVRAFKS VGGEPFFVAR ADGSYLFDVD GNRYIDYVGS 

        70         80         90        100        110        120 
WGPMIAGHNH PAVREAVERA IRDGLSFGAP CAAEVTMAET ITGLVPSCEM VRMVNSGTEA 

       130        140        150        160        170        180 
TLSAVRLARG ATGRNRIIKF EGCYHGHGDS FLVKAGSGML TLGVPTSPGV PAGLSELTAT 

       190        200        210        220        230        240 
LSFNDFEGAT ALFDEIGPEV AAVIIEPVVG NANCIPPQAG YLQHLRTLCT RHGALLIFDE 

       250        260        270        280        290        300 
VMTGFRVALG GAQAHYGVTP DLSTFGKIIG GGMPVGAYGG RRDLMEQIAP AGPIYQAGTL 

       310        320        330        340        350        360 
SGNPVAMAAG LAMLELVQEP GFHMRLSEAT SALCEGLKDA ARTAGIAVTT NQVGGMFGLF 

       370        380        390        400        410        420 
FTDDIVESYA QATACDITSF NRFFHAMLQR GVYLAPSAYE AGFMSSAHDA TVIEATLAAA 


RDAFADVAR 

« Hide

References

[1]"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."
Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.
Jpn. Agric. Res. Q. 39:275-287(2005)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF 311018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008229 Genomic DNA. Translation: BAE67883.1.
RefSeqYP_450157.1. NC_007705.1.

3D structure databases

ProteinModelPortalQ2P6E4.
SMRQ2P6E4. Positions 1-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342109.XOO_1128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE67883; BAE67883; BAE67883.
GeneID3858834.
KEGGxom:XOO_1128.
PATRIC24111689. VBIXanOry49434_1276.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000263533.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycXORY342109:GIX9-1152-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_XANOM
AccessionPrimary (citable) accession number: Q2P6E4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 62 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