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

Q2JMP7 (GSA_SYNJB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:CYB_1012
OrganismSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321332 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length436 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 – 436436Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243629

Amino acid modifications

Modified residue2761N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2JMP7 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: C86B8D6FE5F30730

FASTA43646,729
        10         20         30         40         50         60 
MTSTLHSTSF NTTRSKQVFA RAQSLMPGGV SSPVRAFKSV GGDPVVFDRV SGAYAWDVDG 

        70         80         90        100        110        120 
NQYIDYIGSW GPAIVGHAHP EVIEALRRAL EKGTSFGAPC VLENELAERV IEAVPSVEMV 

       130        140        150        160        170        180 
RFVNSGTEAC MAVLRLMRAY TGREKVIKFE GCYHGHADMF LVKAGSGVAT LGLPDSPGVP 

       190        200        210        220        230        240 
KAATSATLTA PYNDLEAVKA LFEQHPDSIA GVILEPVVGN AGFIPPQPGF LEGLRDLTQK 

       250        260        270        280        290        300 
YGALLVFDEV MTGFRISYGG VQAKFGVIPD LTTLGKVIGG GLPVGAYGGR REIMEMVAPA 

       310        320        330        340        350        360 
GPMYQAGTLS GNPLAMTAGI QTLDILRRPG TYEYLERITE KLATGLLQIA RETGHEMCGG 

       370        380        390        400        410        420 
YLPGMFGFFF TAGPVRNYEE AKTSDLQKFA RFHRGMLERG VYLAPSQFEA GFTSLAHTEA 

       430 
DVEKTLAAAR EVLSTL 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000240 Genomic DNA. Translation: ABD01990.1.
RefSeqYP_477253.1. NC_007776.1.

3D structure databases

ProteinModelPortalQ2JMP7.
SMRQ2JMP7. Positions 10-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321332.CYB_1012.

Proteomic databases

PRIDEQ2JMP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD01990; ABD01990; CYB_1012.
GeneID3900384.
KEGGcyb:CYB_1012.
PATRIC23804332. VBISynSp29577_1023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP321332:GH1B-1012-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_SYNJB
AccessionPrimary (citable) accession number: Q2JMP7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 65 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