Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3ALU9 (GSA_SYNSC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:Syncc9605_0659
OrganismSynechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]
Taxonomic identifier110662 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243627

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ALU9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 796454BDC0D7964E

FASTA42844,785
        10         20         30         40         50         60 
MNTSHSQAIF GAAQALMPGG VSSPVRAFKS VGGQPIVFDR VKGPYAWDVD GNKYIDYIGS 

        70         80         90        100        110        120 
WGPAICGHAH PEVIAALQEA IEKGTSFGAP CALENTLAEM VIDAVPSVEM VRFVNSGTEA 

       130        140        150        160        170        180 
CMAVLRLIRA YTGRDKVIKF EGCYHGHADM FLVKAGSGVA TLGLPDSPGV PRSTTANTLT 

       190        200        210        220        230        240 
APYNDLEAVK ALFAENPEAI AGVILEPIVG NAGFIQPEPG FLEGLRELTK EHGALLVFDE 

       250        260        270        280        290        300 
VMTGFRISYG GAQAHFGVTP DLTTMGKVIG GGLPVGAYGG RADIMGMVAP AGPMYQAGTL 

       310        320        330        340        350        360 
SGNPLAMTAG IKTLELLKQP GTYEKLTATT QKLVAGIKDA AQSAGMSITA ASVSAMFGFF 

       370        380        390        400        410        420 
LCEGPVRNFE EAKATDSERF GKLHRAMLEH GVYLAPSAFE AGFTSLAHSE ADIEATINAF 


RESFAAVA 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9605."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9605.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000110 Genomic DNA. Translation: ABB34433.1.
RefSeqYP_380988.1. NC_007516.1.

3D structure databases

ProteinModelPortalQ3ALU9.
SMRQ3ALU9. Positions 3-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING110662.Syncc9605_0659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB34433; ABB34433; Syncc9605_0659.
GeneID3736584.
KEGGsyd:Syncc9605_0659.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycSSP110662:GJ7R-687-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...

Entry information

Entry nameGSA_SYNSC
AccessionPrimary (citable) accession number: Q3ALU9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 66 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