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Q8DLK8 (GSA_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:tlr0479
OrganismThermosynechococcus elongatus (strain BP-1)
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP MF_00375

Cofactor

Pyridoxal phosphate.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP MF_00375

Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP MF_00375

Subunit structure

Homodimer By similarity. HAMAP MF_00375

Subcellular location

Cytoplasm Potential HAMAP MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Sequence caution

The sequence BAC08031.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Glutamate-1-semialdehyde 2,1-aminomutase HAMAP MF_00375
PRO_0000120460

Amino acid modifications

Modified residue2771N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

1 .......................................................... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8DLK8 [UniParc].

Last modified June 20, 2003. Version 2.
Checksum: 5FDD56F62A179C23

FASTA43746,450
        10         20         30         40         50         60 
MRELTLTTTV FQTTKSQEIF AAAQKLMPGG VSSPVRAFKS VGGQPIVFDH VKGAHIWDVD 

        70         80         90        100        110        120 
GNQYIDYVGS WGPAIVGHAH PEVIDALHAA LEKGTSFGAP CLLENILAEM VIAAVPSVEM 

       130        140        150        160        170        180 
VRFVNSGTEA CMAVLRLMRA YTQREKVIKF EGCYHGHADM FLVKAGSGVA TLGLPDSPGV 

       190        200        210        220        230        240 
PKATTAATLT APYNDLEAVS RLFEQYPNDI AGVILEPVVG NAGFIPPDAG FLEGLRELTK 

       250        260        270        280        290        300 
QYGALLVFDE VMTGFRIAYG GAQEKFGVTP DLTTLGKVIG GGLPVGAYGG RAEIMKMVAP 

       310        320        330        340        350        360 
AGPVYQAGTL SGNPLAMTAG IKTLEILSRP GSYEHLDRIT GKLVQGLLDA AREFGHEVCG 

       370        380        390        400        410        420 
GHISGMFGLF FTAGPVTNYE QAKQSDLKKF AAFHRGMLEQ GIYLAPSQFE AGFTSLAHTE 

       430 
ADIERTIAAA RTVLSQL

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000039 Genomic DNA. Translation: BAC08031.1. Different initiation.
RefSeqNP_681269.2. NC_004113.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFBX-ray2.85A27-437[»]
ProteinModelPortalQ8DLK8.
SMRQ8DLK8. Positions 11-437.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8DLK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1012458.
GenomeReviewsGene locus tlr0479 in contig BA000039_GR.
KEGGtel:tlr0479.
NMPDRfig|197221.1.peg.478.
PATRIC23926202. VBITheElo119873_0504.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHBG725944.
OMATYNDLDS.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycTELO197221:TLR0479-MONOMER.

Family and domain databases

HAMAPMF_00375. HemL_aminotrans_3.
[Tree]
InterProIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK01845.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF5. PTHR11986:SF5. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00713. HemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_THEEB
AccessionPrimary (citable) accession number: Q8DLK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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