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B9DZG0 (GSA_CLOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:CKR_0584
OrganismClostridium kluyveri (strain NBRC 12016) [Complete proteome] [HAMAP]
Taxonomic identifier583346 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length422 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.

Sequence caution

The sequence BAH05635.1 differs from that shown. Reason: Erroneous initiation.

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 – 422422Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382296

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B9DZG0 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: FAEAEDE075C78EA7

FASTA42246,726
        10         20         30         40         50         60 
MRNDKIFEES KLYMPGGVNS PVRAFKDVPL NPPVIKKGRG AYIYDEDGNE YIDFVCSWGP 

        70         80         90        100        110        120 
MILGHCDEDV VNAIKYTSEN AISFGATTKI ELELSKYICT TMDNIEMIRM VNSGTEATMS 

       130        140        150        160        170        180 
AVKLARGYTR RNKIIKFSGC YHGHFDDFLV EAGSGVMTEG IPGSAGVPKD SIKNTIIAEY 

       190        200        210        220        230        240 
NNLEDVKNIF NKYGSDTAAI IVEPVAGNMG VIPGRIDFLK GLRKLCDEYG SLLIFDEVMS 

       250        260        270        280        290        300 
GFRVAYKGAQ SLYGIKPDIT TMAKIMGGGL PCGAYGGRKD IMENLSPLGP VYQAGTMSGN 

       310        320        330        340        350        360 
PIVMAAGLAT LKKLNENPDY YVKLEKLGKK LEKGIKQISK DKNIPMVINR CGAMFSIFFT 

       370        380        390        400        410        420 
SDSEVKNYKD ARKCDTTIFA KFFQHMLERG IYIAPSQFEA IFLNVKHTEE HIDKFLQAVN 


TF 

« Hide

References

[1]"Complete genome sequence of Clostridium kluyveri and comparative genomics of Clostridia species."
Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A., Yukawa H.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 12016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009049 Genomic DNA. Translation: BAH05635.1. Different initiation.
RefSeqYP_002471049.1. NC_011837.1.

3D structure databases

ProteinModelPortalB9DZG0.
SMRB9DZG0. Positions 3-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING583346.CKR_0584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH05635; BAH05635; CKR_0584.
GeneID7274061.
KEGGckr:CKR_0584.
PATRIC19470918. VBICloKlu118830_0718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCKLU583346:GJNQ-617-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 nameGSA_CLOK1
AccessionPrimary (citable) accession number: B9DZG0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 39 of the entry and version 2 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