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B7HE93 (GSA2_BACC4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:BCB4264_A4579
OrganismBacillus cereus (strain B4264) [Complete proteome] [HAMAP]
Taxonomic identifier405532 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

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_0000382270

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7HE93 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 8D47EE5E83A0CAC5

FASTA42946,021
        10         20         30         40         50         60 
MKKFDKSIAA FEEAQDLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI DGNEYIDYVL 

        70         80         90        100        110        120 
SWGPLIHGHA NDRVVEALKS VAERGTSFGA PTEIENKLAK LVIERVPSIE IVRMVNSGTE 

       130        140        150        160        170        180 
ATMSALRLAR GYTGRNKILK FIGCYHGHGD SLLIKAGSGV ATLGLPDSPG VPEGVAKNTI 

       190        200        210        220        230        240 
TVAYNDLESV KYAFEQFGDD IACVIVEPVA GNMGVVPPQP GFLEGLREVT EQNGALLIFD 

       250        260        270        280        290        300 
EVMTGFRVAY NCGQGYYGVT PDLTCLGKVI GGGLPVGAYG GKAEIMRQVA PSGPIYQAGT 

       310        320        330        340        350        360 
LSGNPLAMAA GYETLVQLTP ESYVEFERKA EMLEAGLRKA AEKHGIPHHI NRAGSMIGIF 

       370        380        390        400        410        420 
FTDEPVINYD AAKSSNLEFF AAYYREMVEQ GVFLPPSQFE GLFLSTAHSD ADIEATIAAA 


EIAMSKLKA 

« Hide

References

[1]"Genome sequence of Bacillus cereus B4264."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001176 Genomic DNA. Translation: ACK61561.1.
RefSeqYP_002369268.1. NC_011725.1.

3D structure databases

ProteinModelPortalB7HE93.
SMRB7HE93. Positions 1-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405532.BCB4264_A4579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK61561; ACK61561; BCB4264_A4579.
GeneID7099722.
KEGGbcb:BCB4264_A4579.
PATRIC18881047. VBIBacCer117876_4429.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycBCER405532:GI1K-4536-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_BACC4
AccessionPrimary (citable) accession number: B7HE93
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 44 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