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B0CC57 (GSA_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:AM1_0549
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris

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_1000079914

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CC57 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: DD9B362193EC2217

FASTA43245,617
        10         20         30         40         50         60 
MLTDTLNTTK SEEIFAAAQK LMPGGVSSPV RAFKSVGGQP IVFDRVKGAH VWDVDGNQYI 

        70         80         90        100        110        120 
DYVGTWGPAI CGHAHPEVLT ALKEALDKGT SFGAPCLLEN VLAEMVIDAV PSVEVVRFVN 

       130        140        150        160        170        180 
SGTEACMSVL RLMRAFTGRE KVIKFEGCYH GHADMFLVKA GSGVATLGLP DSPGVPKSVT 

       190        200        210        220        230        240 
GNTLTAPYND LQSVQALFSQ HPDQIAGVIL EPVVGNAGFI PPDAGFLEGL REITKENGAL 

       250        260        270        280        290        300 
LVFDEVMTGF RISYGGAQEK FGITPDLTTL GKVIGGGLPV GAYGGRRDIM SMVAPAGPMY 

       310        320        330        340        350        360 
QAGTLSGNPL AMTAGIKTLE LLRRSGTYDQ LDRVTGKLIS GLLQIAREAG HEVCGGHING 

       370        380        390        400        410        420 
MFGMFFAPGP VHSYDDAKAA DAAKFAKFHR GMLEQGVYLA PSQFEAGFTS LAHTDADIDQ 

       430 
TLEAAKVVLA NI 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW25599.1.
RefSeqYP_001514913.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CC57.
SMRB0CC57. Positions 6-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING329726.AM1_0549.

Proteomic databases

PRIDEB0CC57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW25599; ABW25599; AM1_0549.
GeneID5679377.
KEGGamr:AM1_0549.
PATRIC20615632. VBIAcaMar40141_0468.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-542-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_ACAM1
AccessionPrimary (citable) accession number: B0CC57
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 52 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