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A9KSC7 (GSA2_CLOPH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Cphy_1789
OrganismClostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]
Taxonomic identifier357809 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length426 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382299

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KSC7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 4D10EB488D37D7A2

FASTA42646,860
        10         20         30         40         50         60 
MTKSEQLFER AVKHLPGGVN SPVRAFLSVG GSPRFIESAD GAYIYDVDGN KYIDYINSWG 

        70         80         90        100        110        120 
PMILGHNHEV IRTAVIEAAQ KGLSYGAATE AEVEMAELLC EIVPCFEMVR MVNSGTEAVM 

       130        140        150        160        170        180 
SAIRAARGYT KRNKIIKFEG CYHGHSDGLL VKAGSGVMVA GIPDSMGVPS NCVKDTLQAK 

       190        200        210        220        230        240 
YNNLDSVIEL FKQNKDEIAA IIVEPVAANM GVVLPEEGFL EGLRELCTKH GALLIFDEVI 

       250        260        270        280        290        300 
TGFRLSLSGA QGYYNIIPDL ATFGKIIGGG MPVGCYGGRR EIMEMVAPVG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGMA QLKYLKEHPE VYTKINELGE YFRNKVNELF DKYNIKYQVS GVGSLACIFF 

       370        380        390        400        410        420 
ADSRVTDYET AKLADTKEFA RYFRFMLEHG IYIAPAQFEA MFFSNAHTYQ DIEDTLLVIE 


QYLKIQ 

« Hide

References

[1]"Complete genome sequence of Clostridium phytofermentans ISDg."
Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. expand/collapse author list , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000885 Genomic DNA. Translation: ABX42159.1.
RefSeqYP_001558898.1. NC_010001.1.

3D structure databases

ProteinModelPortalA9KSC7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357809.Cphy_1789.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX42159; ABX42159; Cphy_1789.
GeneID5743078.
KEGGcpy:Cphy_1789.
PATRIC19503222. VBICloPhy16213_1850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAPGFKPDI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycCPHY357809:GHCL-1829-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_CLOPH
AccessionPrimary (citable) accession number: A9KSC7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 54 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