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

B7GH35 (GSA2_ANOFW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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 2

Short name=GSA 2
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name=GSA-AT 2
Gene names
Name:hemL2
Ordered Locus Names:Aflv_0610
OrganismAnoxybacillus flavithermus (strain DSM 21510 / WK1) [Complete proteome] [HAMAP]
Taxonomic identifier491915 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeAnoxybacillus

Protein attributes

Sequence length431 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.

Sequence caution

The sequence ACJ32991.1 differs from that shown. Reason: Erroneous initiation.

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 – 431431Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382251

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7GH35 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 6F6DBDBBAAE864F7

FASTA43146,825
        10         20         30         40         50         60 
MRSYERSKAA YAEAVKLMPG GVNSPVRAFK AVKMDPIFMA RGKGSKIYDI DGNEYIDYVL 

        70         80         90        100        110        120 
SWGPLILGHA NDQVVEALKR VAETGTSFGA PTLIENELAK LVMERMPSIE IIRMVSSGTE 

       130        140        150        160        170        180 
ATMSALRLAR GYTGRNKIVK FEGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPETVAQHTI 

       190        200        210        220        230        240 
TVPYNDLQSV RYAFEKFGED IAAVIVEPVA GNMGVVPPEP GFLQGLRDVT NEYGALLIFD 

       250        260        270        280        290        300 
EVMTGFRVDY YSGQGYYGVT PDLTCLGKVI GGGLPVGAYG GRADIMEKIA PSGPIYQAGT 

       310        320        330        340        350        360 
LSGNPMAMTA GYETLRQLTP ETYEAFKKKA NRLAEGLSEA AKAYHIPHTI NQAGSMIGMF 

       370        380        390        400        410        420 
FTNERVTNYE TAKTSNLDLF ARYYQEMANE GIFLPPSQFE GMFLSTAHTD EDIEKTIEAA 

       430 
RRAFAKMSDC L 

« Hide

References

[1]"Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1."
Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.
Genome Biol. 9:R161.1-R161.16(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21510 / WK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000922 Genomic DNA. Translation: ACJ32991.1. Different initiation.
RefSeqYP_002314976.1. NC_011567.1.

3D structure databases

ProteinModelPortalB7GH35.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING491915.Aflv_0610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ32991; ACJ32991; Aflv_0610.
GeneID7036867.
KEGGafl:Aflv_0610.
PATRIC20953033. VBIAnoFla45531_0627.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycAFLA491915:GHEO-685-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 nameGSA2_ANOFW
AccessionPrimary (citable) accession number: B7GH35
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 42 of the entry and version 2 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