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A5D3M2 (GSA_PELTS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:PTH_0979
OrganismPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) [Complete proteome] [HAMAP]
Taxonomic identifier370438 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum

Protein attributes

Sequence length434 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 – 434434Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000079927

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5D3M2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 7C827FCAE7964D15

FASTA43446,033
        10         20         30         40         50         60 
MYKGFDRSVS LYRQACKVIP GGVNSPVRAF KAVGLNPVFV KKGEGARIYD FDDNEYIDYV 

        70         80         90        100        110        120 
CSWGPLILGH RHPRVVGALE RCLNEVGTSF GAPTELENIL AEMIVEAVPS IEMVRLVNSG 

       130        140        150        160        170        180 
TEAAMSALRL ARGYTGRNKI VKFEGCYHGH ADFLLIKAGS GALTFGVPTS PGIPAAAAAG 

       190        200        210        220        230        240 
TIVARYNDLA GLEEIFKLEG EDIAAVIVEP VAGNMGVVPP APGFLEGLRN LTARYGSLLI 

       250        260        270        280        290        300 
FDEVITGFRL AYGGAQELYG VAPDLTCLGK VIGGGLPVGA YGGRREIMEQ VAPSGPVYQA 

       310        320        330        340        350        360 
GTLSGNPLAV SAGIATLEVL KQPGVYGRLE QTAAALEDAL KQAARQTGAE VCFNRAGSML 

       370        380        390        400        410        420 
CAFFTGEEVK DYASACTSDT ARYAAFFRSM LEQGVYLAPS QFEAAFVSLA HGKEEIERTA 

       430 
EAARHAFKAA VEQK 

« Hide

References

[1]"The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13744 / JCM 10971 / SI.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009389 Genomic DNA. Translation: BAF59160.1.
RefSeqYP_001211529.1. NC_009454.1.

3D structure databases

ProteinModelPortalA5D3M2.
SMRA5D3M2. Positions 5-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370438.PTH_0979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF59160; BAF59160; PTH_0979.
GeneID5138980.
KEGGpth:PTH_0979.
PATRIC22908989. VBIPelThe8413_1099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPTHE370438:GCGQ-1015-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_PELTS
AccessionPrimary (citable) accession number: A5D3M2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 52 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