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P24630 (GSA_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. 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:syc0881_c
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

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

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. HAMAP-Rule MF_00375

Subunit structure

Homodimer.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

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

Sequence caution

The sequence BAD79071.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 433432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120461

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00375

Experimental info

Sequence conflict511Y → I Ref.1
Sequence conflict511Y → I Ref.2
Sequence conflict1081I → N Ref.1
Sequence conflict1081I → N Ref.2
Sequence conflict133 – 1342LM → VV Ref.1
Sequence conflict133 – 1342LM → VV Ref.2
Sequence conflict1721D → S Ref.1
Sequence conflict1721D → S Ref.2
Sequence conflict1791S → K Ref.1
Sequence conflict1791S → K Ref.2
Sequence conflict1871A → T Ref.1
Sequence conflict1871A → T Ref.2
Sequence conflict3271A → G Ref.1
Sequence conflict3271A → G Ref.2

Secondary structure

.................................................................................. 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24630 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 83585133A666B923

FASTA43346,116
        10         20         30         40         50         60 
MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA YAWDVDGNRY 

        70         80         90        100        110        120 
IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE NVLAEMVIDA VPSIEMVRFV 

       130        140        150        160        170        180 
NSGTEACMAV LRLMRAYTGR DKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPKST 

       190        200        210        220        230        240 
TANTLTAPYN DLEAVKALFA ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA 

       250        260        270        280        290        300 
LLVFDEVMTG FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM 

       310        320        330        340        350        360 
YQAGTLSGNP LAMTAGIKTL ELLRQPATYE YLDQITKRLS DGLLAIAQET GHAACGGQVS 

       370        380        390        400        410        420 
GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL APSQFEAGFT SLAHTEEDID 

       430 
ATLAAARTVM SAL 

« Hide

References

« Hide 'large scale' references
[1]"Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli."
Grimm B., Bull A., Breu V.
Mol. Gen. Genet. 225:1-10(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of Synechococcus. Deletion of a tripeptide close to the NH2 terminus and internal amino acid substitution."
Grimm B., Smith A.J., Kannangara C.G., Smith M.
J. Biol. Chem. 266:12495-12501(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[4]"Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus."
Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.
Carlsberg Res. Commun. 54:67-79(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-17.
[5]"Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity."
Hennig M., Grimm B., Contestabile R., John R.A., Jansonius J.N.
Proc. Natl. Acad. Sci. U.S.A. 94:4866-4871(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53695 Genomic DNA. Translation: CAA37733.1.
AP008231 Genomic DNA. Translation: BAD79071.1. Different initiation.
PIRS13326.
RefSeqYP_171591.2. NC_006576.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSAX-ray2.40A/B2-433[»]
3FQ7X-ray2.15A/B7-433[»]
3FQ8X-ray2.00A/B7-433[»]
3FQAX-ray2.35A/B7-433[»]
3GSBX-ray3.00A/B2-433[»]
4GSAX-ray2.50A/B2-433[»]
ProteinModelPortalP24630.
SMRP24630. Positions 7-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc0881_c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD79071; BAD79071; syc0881_c.
GeneID3199069.
KEGGsyc:syc0881_c.
PATRIC32487518. VBISynElo117686_1027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-897-MONOMER.
UniPathwayUPA00251; UER00317.
UPA00668.

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...

Other

EvolutionaryTraceP24630.

Entry information

Entry nameGSA_SYNP6
AccessionPrimary (citable) accession number: P24630
Secondary accession number(s): Q5N3P9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 114 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways