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

B1XIT5 (GSA_SYNP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:SYNPCC7002_A2206
OrganismSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]
Taxonomic identifier32049 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length432 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121927

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XIT5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: E3FF770E7C1064B3

FASTA43246,096
        10         20         30         40         50         60 
MVTTALNTTK SEEIFSAAQK LMPGGVSSPV RAFKSVGGQP IVFDRVKGSR VWDVDGNEYI 

        70         80         90        100        110        120 
DYVGTWGPAI CGHANDEVNA ALRETLEKGT SFGAPCLKEN ILAEMVINAV PSIEMVRFVN 

       130        140        150        160        170        180 
SGTEACMSVL RLMRAFTGRE KIIKFEGCYH GHADMFLVQA GSGVATLGLP DSPGVPKTTT 

       190        200        210        220        230        240 
AATLTAPYND LEAVKKLFAE NPGEIAGVIL EPVVGNSGFV LPDAGFLEGL REITKEHDAL 

       250        260        270        280        290        300 
LVFDEVMTGF RISYGGAQEK FGVTPDLTTL GKVIGGGLPV GAYGGRKDIM SMVAPAGPMY 

       310        320        330        340        350        360 
QAGTLSGNPL AMTAGIKTLE LLQRPGMYGQ LETITKKLID GLLSIAREAG HEVTGGNISG 

       370        380        390        400        410        420 
MFGMFFTGEP VRNYEDAKKS DLHKFSRYHR GMLEQGIYLA PSQFEAGFTS LAHTDEDIEK 

       430 
TLAAAKVVLN NL 

« Hide

References

[1]"Complete sequence of Synechococcus sp. PCC 7002."
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27264 / PCC 7002 / PR-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000951 Genomic DNA. Translation: ACB00187.1.
RefSeqYP_001735442.1. NC_010475.1.

3D structure databases

ProteinModelPortalB1XIT5.
SMRB1XIT5. Positions 6-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING32049.SYNPCC7002_A2206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB00187; ACB00187; SYNPCC7002_A2206.
GeneID6055724.
KEGGsyp:SYNPCC7002_A2206.
PATRIC23819050. VBISynSp37135_2458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSSP32049:GKF7-2207-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_SYNP2
AccessionPrimary (citable) accession number: B1XIT5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 47 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