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B2UNE3 (GSA_AKKM8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Amuc_0417
OrganismAkkermansia muciniphila (strain ATCC BAA-835) [Complete proteome] [HAMAP]
Taxonomic identifier349741 [NCBI]
Taxonomic lineageBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia

Protein attributes

Sequence length426 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382245

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2UNE3 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 6FF01ED031CA59ED

FASTA42646,335
        10         20         30         40         50         60 
MNQSAQLFSR ARSVIPGGVN SPVRAFRNVD GDPFFVQSAK GAYITDADGR QLIDYIGTWG 

        70         80         90        100        110        120 
PAILGHAPQP VLDAVHAAVD RGLGYGIPAP AEVDMAEMIT DMVPSVEKVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRRKIIKFIG CYHGHVDSLL VAAGSGALTF GEPDSAGVPR EMTQLTLTVP 

       190        200        210        220        230        240 
YNDREAVKKA FELHGSDIAA VILEPFPANA GLYFPQNDFL HFLREITLRH DTLLIFDEVM 

       250        260        270        280        290        300 
TGFRVAPGGV QQLYGITPDL TCMGKVIGGG LPVGAFGGRS EIMDCLSPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGLA QLRELLKGNA YERLEQLGAR MEEGIREALK KHGRNYTFHR AGSMFCLFFT 

       370        380        390        400        410        420 
EEEVYNLESA QKASKKLFKS FFWNMLEQGV YFAPSPYETG FISTAHTEED IDRTVEAVRI 


SLSRLG 

« Hide

References

[1]"Complete sequence of Akkermansia muciniphila ATCC BAA-835."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. expand/collapse author list , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-835.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001071 Genomic DNA. Translation: ACD04255.1.
RefSeqYP_001877036.1. NC_010655.1.

3D structure databases

ProteinModelPortalB2UNE3.
SMRB2UNE3. Positions 3-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349741.Amuc_0417.

Proteomic databases

PRIDEB2UNE3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD04255; ACD04255; Amuc_0417.
GeneID6274835.
KEGGamu:Amuc_0417.
PATRIC20833434. VBIAkkMuc16855_0473.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycAMUC349741:GHZ7-437-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_AKKM8
AccessionPrimary (citable) accession number: B2UNE3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 49 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