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Q2LVW6 (GSA_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:SYNAS_23480
ORF Names:SYN_00583
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length432 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243633

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LVW6 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: BC1AB2B17269FBDE

FASTA43246,456
        10         20         30         40         50         60 
MTKSLSEQLF ETAEGLLPGG VNSPVRAFRA VGGVPRFIDR AEGSRIYDID GREYIDYVGS 

        70         80         90        100        110        120 
WGPMILGHSH PQVVEAIRKA VERGTSYGAP TPGEIALART IIEAFPSMEM IRMVSSGTEA 

       130        140        150        160        170        180 
VMSAIRLARG FTGRDKILKF EGCYHGHGDS LLVKAGSGVA TLGIPGSPGV PACLAELTIT 

       190        200        210        220        230        240 
VPFNSNEAFR KAVDRHGKEL ACVIVEPVAA NMGVVNPRPG FLETLRELTR KAGIVLIFDE 

       250        260        270        280        290        300 
VITGFRLAYG GFQKLCRLEP DLTCLGKIIG GGLPVGAFGG KRTIMDFLAP NGPVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMSAG LATLETLRSR RDDYAALDRR TADLCAAMGK LFRTAELPVR INRAGSLFTV 

       370        380        390        400        410        420 
FFTDSDVFDY ETASHCNLER YARFFKGMLD RGVYLAPSAF EAAFVSFAHS DEDLEKTLQA 

       430 
CAETIKTLGG NP 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC78227.1.
RefSeqYP_462395.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LVW6.
SMRQ2LVW6. Positions 1-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_00583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC78227; ABC78227; SYN_00583.
GeneID3883628.
KEGGsat:SYN_00583.
PATRIC23865506. VBISynAci70500_2535.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSACI56780:GHXT-2397-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_SYNAS
AccessionPrimary (citable) accession number: Q2LVW6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 21, 2006
Last modified: February 19, 2014
This is version 61 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