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A1AVQ1 (GSA_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Rmag_0222
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

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

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen 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_0000300943

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AVQ1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 73FB004154C777A6

FASTA42845,699
        10         20         30         40         50         60 
MNQSETLFAQ AKTVIPGGVN SPVRAFNGVG GSPIFFTRGE GAYLFDEDDK KYIDYVASWG 

        70         80         90        100        110        120 
SMILGHTNQA VIIAVKTTLE NGLGFGAPTQ IETKLAEKVC ELMPSIELVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGHT GRDKIIKFEG CYHGHSDSLL IKAGSGALTL GVPTSPGVPK DFAKHTLTLE 

       190        200        210        220        230        240 
YNNIDQVCEV LSEVGAEVAC IIVEPVAGNM NCIPPIDGFL QVLRELCDEY GVILVFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAFYNVKPDL TTLGKVIGGG LPVGAFGGKR EIMQSIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPISMSAGLV MLNVLSKDEN FYTILNTKVQ KLTKGILAKA KENNIGMTAN VVGGMFGLFF 

       370        380        390        400        410        420 
TDSQSVTNFK ETSQCNIELF KKFFHLMLAE GVYMAPSAYE AGFVSSAHSD TDIQNTIDAA 


GRAFIKLT 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL02008.1.
RefSeqYP_903479.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AVQ1.
SMRA1AVQ1. Positions 2-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0222.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02008; ABL02008; Rmag_0222.
GeneID4554897.
KEGGrma:Rmag_0222.
PATRIC32000039. VBICanRut45856_0248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCRUT413404:GHM7-231-MONOMER.
UniPathwayUPA00251; UER00317.

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_RUTMC
AccessionPrimary (citable) accession number: A1AVQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 51 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