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A7Z7A2 (GSA2_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:RBAM_025180
OrganismBacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC 10A6 / FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length429 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382258

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z7A2 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 002323C35CF15D82

FASTA42946,139
        10         20         30         40         50         60 
MRSYEKSKAA FKEAQKLMPG GVNSPVRAFK SVDMDPIFMQ RGKGSKIFDI DGNEYIDYVL 

        70         80         90        100        110        120 
SWGPLILGHT NDRVVESLKK VAENGTSFGA STEVENELAK LVIDRVPSVE IVRMVSSGTE 

       130        140        150        160        170        180 
ATMSALRLAR GYTGRNKILK FEGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPEGIAMNTI 

       190        200        210        220        230        240 
TVPYNDLESV ALAFREYGED IAGVIVEPVA GNMGVVPPQE GFLQGLRDMT EQYGALLIFD 

       250        260        270        280        290        300 
EVMTGFRVDY NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKADIMERIA PSGPIYQAGT 

       310        320        330        340        350        360 
LSGNPLAMTA GLETLQQLTP ESYQEFVKKG DMLEEGISKA AAAHGIPHTF NRAGSMIGFF 

       370        380        390        400        410        420 
FTNEPVINYE AAKSSDLKLF AKYYKGMADA GVFLPPSQFE GLFLSTAHTM EDIENTIQAA 


EKVFQAISR 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 23117 / BGSC 10A6 / FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS74878.1.
RefSeqYP_001422109.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z7A2.
SMRA7Z7A2. Positions 5-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326423.RBAM_025180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS74878; ABS74878; RBAM_025180.
GeneID5460782.
KEGGbay:RBAM_025180.
PATRIC18750154. VBIBacAmy31356_2552.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAMY326423:GCM4-2516-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_BACA2
AccessionPrimary (citable) accession number: A7Z7A2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 55 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