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C0ZAH4 (GSA2_BREBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:BBR47_18060
OrganismBrevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599) [Complete proteome] [HAMAP]
Taxonomic identifier358681 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus

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_0000382285

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0ZAH4 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 77DF96DC90C532F8

FASTA42945,955
        10         20         30         40         50         60 
MNREKSTQLF AEAQHYIPGG VNSPVRAFKS VGGNPVYIEK GEGSRIFDVD GNSYIDYIGS 

        70         80         90        100        110        120 
WGPLILGHAH PRVLAAITEV AALGTSFGAP TERETEMAKL VCEIVPSVEV VRMVNSGTEA 

       130        140        150        160        170        180 
TMSALRLARG YTRRNKIMKF EGCYHGHADS LLIKAGSGVA TLGLPDSPGV PEGTAHNTIT 

       190        200        210        220        230        240 
VPYNDLESVK LAFEAFGDDL AAVIVEPIGG NMGVVPPQPG FLEGLREITE KHGTLLIFDE 

       250        260        270        280        290        300 
VMTGFRVALG GAQELYGITP DLTTMGKVIG GGLPVGAYGG KREIMQQVAP AGPIYQAGTL 

       310        320        330        340        350        360 
SGNPLAMAAG LTTLQELSKP GAYERLEKMS ARLAEGLADN AKKLGIPHTL NRVGSMVCLF 

       370        380        390        400        410        420 
FTETPVINYE TAKTSDLERF SAYFSYLLEE GVMIPPSQFE GMFVSLAHTD EDIERTIEAS 


YQAMKKAFK 

« Hide

References

[1]"Brevibacillus brevis strain 47, complete genome."
Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H. expand/collapse author list , Udaka S., Tanikawa S., Fujita N.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 47 / JCM 6285 / NBRC 100599.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008955 Genomic DNA. Translation: BAH42783.1.
RefSeqYP_002771287.1. NC_012491.1.

3D structure databases

ProteinModelPortalC0ZAH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING358681.BBR47_18060.

Proteomic databases

PRIDEC0ZAH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH42783; BAH42783; BBR47_18060.
GeneID7719682.
KEGGbbe:BBR47_18060.
PATRIC21233920. VBIBreBre96763_1794.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMASQFETIF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycBBRE358681:GHYS-1919-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_BREBN
AccessionPrimary (citable) accession number: C0ZAH4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 40 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