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A8FFU9 (GSA2_BACP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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 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:BPUM_2453
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382278

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FFU9 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 3634116D497495E0

FASTA43046,722
        10         20         30         40         50         60 
MGRSYEKSKQ AFEEAQHLMP GGVNSPVRAF KSVNTDPIFM ERGKGAKIYD IDGNEYIDYV 

        70         80         90        100        110        120 
LSWGPLILGH TNDRVVESIQ RVAEKGTSFG ASTLVENELA KLVSERVPSI EVIRMVSSGT 

       130        140        150        160        170        180 
EATMSALRLA RGFTGRNKIV KFEGCYHGHG DSLLIKAGSG VATLGLPDSP GVPEGTASNT 

       190        200        210        220        230        240 
ITVPYNDLES IQVAFQEFGD DIAGVIVEPV AGNMGVVPPQ DGFLQGLRDI TEQYGALLIF 

       250        260        270        280        290        300 
DEVMTGFRVD YHCAQGYFGV TPDLTCLGKV IGGGLPVGAY GGRADIMRQI APSGPIYQAG 

       310        320        330        340        350        360 
TLSGNPLAMT AGLETLKQLT PESYEEFRRK GDRLEEGISN AAKTHGIPLT FNRAGSMIGF 

       370        380        390        400        410        420 
FFTDEEVINY DIAKNADLAL FAEFYKEMAD HGIFLPPSQF EGLFLSTAHT DEDIEYTIET 

       430 
VEKVFQKLRR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000813 Genomic DNA. Translation: ABV63116.1.
RefSeqYP_001487676.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8FFU9.
SMRA8FFU9. Positions 6-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315750.BPUM_2453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV63116; ABV63116; BPUM_2453.
GeneID5621722.
KEGGbpu:BPUM_2453.
PATRIC18968828. VBIBacPum16546_2509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBPUM315750:GH6N-2510-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_BACP2
AccessionPrimary (citable) accession number: A8FFU9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: November 13, 2007
Last modified: February 19, 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