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Q55665 (GSA_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:gsa
Ordered Locus Names:sll0017
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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 BAA10185.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Glutamate-1-semialdehyde 2,1-aminomutase HAMAP MF_00375
PRO_0000120462

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55665 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 467064245487F923

FASTA43345,892
        10         20         30         40         50         60 
MVNATPFITT KSEEIFAAAQ HLMPGGVSSP VRAFKSVGGQ PIVFDRVEGA QIWDVDGNQY 

        70         80         90        100        110        120 
IDYVGTWGPA ICGHAHPDVI SALKQALDKG TSFGAPCAQE NVLAEMVIDA VPSIEMVRFV 

       130        140        150        160        170        180 
NSGTEACMSV LRLMRAFTGR EKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPSNT 

       190        200        210        220        230        240 
TKATLTAPYN DLEAVKALFV ENPDSIAGVI LEPVVGNAGF ILPDAGFLEG LRELTKEYGA 

       250        260        270        280        290        300 
LLVFDEVMTG FRVSYGGAQA RFGITPDLTT LGKVIGGGLP VGAYGGREEI MAMVAPAGPM 

       310        320        330        340        350        360 
YQAGTLSGNP LAMTAGIKTL EILQKPGSYE YLDKITKRLV DGLLAAAQDA GHEVCGGSIS 

       370        380        390        400        410        420 
AMFGIFFAPG PVRNYEDAKL ADTNKFARFH RGMLERGIYL APSQYEAGFP SLAHTQEQID 

       430 
QTIAVAKEVF ATL 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10185.1. Different initiation.
PIRS76333.
RefSeqNP_442115.2. NC_000911.1.

3D structure databases

ProteinModelPortalQ55665.
SMRQ55665. Positions 7-433.
ModBaseSearch...

Protein-protein interaction databases

IntActQ55665. 1 interaction.
STRINGQ55665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID952666.
GenomeReviewsGene locus sll0017 in contig BA000022_GR.
KEGGsyn:sll0017.
NMPDRfig|1148.1.peg.2216.
PATRIC23841832. VBISynSp132158_2460.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHBG725944.
OMATYNDLDS.
PhylomeDBQ55665.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycSSP1148:SLL0017-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_SYNY3
AccessionPrimary (citable) accession number: Q55665
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families