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Q97MU2 (GSA_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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:CA_C0099
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [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.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference 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_0000120401

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97MU2 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: E37F273660CDDA2B

FASTA42246,615
        10         20         30         40         50         60 
MTNKEIFEES KEYMPGGVNS PVRAYMDLNI DPPIIKSGKD SHLFDEEGKE YIDFIEAWGP 

        70         80         90        100        110        120 
MILGHKNQKV LNEVKEVLDE GVGFGAPTSL ELKLAKYICT TVDNVEMIRM VNSGTEATMS 

       130        140        150        160        170        180 
AVKLARGYTK RDKIIKFAGC YHGHFDGFLV EAGSGVLTQN IPGSPGVPKG SIENTLIAEY 

       190        200        210        220        230        240 
NNVESVEVLF NKYKDEIAAV IIEPVAGNMG VIPAKKEFLV KLRELCTENQ SILIFDEVMS 

       250        260        270        280        290        300 
GFRVAYKGAQ SLYGVTPDLI TFAKIMGGGF PCGAYGGKKE IMKQLSPLGP VYQAGTMSGN 

       310        320        330        340        350        360 
PVVMAAGYAS LRQLHENPEY YTYMDKLGSK LEAGILEISK EKGIPLVVNR CVNMMTIFFN 

       370        380        390        400        410        420 
KAKEVKSYSD AKASDTKMFA RFAEHMITSG IYVPPSQFEA MFLGVKHTEE DIERFLDVMK 


KL 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK78084.1.
PIRA96912.
RefSeqNP_346744.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97MU2.
SMRQ97MU2. Positions 3-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C0099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK78084; AAK78084; CA_C0099.
GeneID1116282.
KEGGcac:CA_C0099.
PATRIC32034467. VBICloAce74127_0282.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCACE272562:GJIH-108-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_CLOAB
AccessionPrimary (citable) accession number: Q97MU2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2001
Last modified: February 19, 2014
This is version 87 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