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Q1IHV2 (GSA_KORVE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:Acid345_4548
OrganismKoribacter versatilis (strain Ellin345) [Reference proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length431 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 – 431431Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382243

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IHV2 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 22324CA599B78F39

FASTA43145,581
        10         20         30         40         50         60 
MSRKLDRSRE LQKRAEALIP GGVNSPVRAF RAVGGEPPIL VRGEGARVFD ADGNGYIDYV 

        70         80         90        100        110        120 
LSWGPLILGH AFTPVINAIE KAAEKGTSFG ASTPTEADLA EAVVHAMPAI EKIRFVSSGT 

       130        140        150        160        170        180 
EATMSAIRLA RGFTGRKYIV KFEGCYHGHS DSLLVKAGSG VATLGIPGSA GVPDELAQLT 

       190        200        210        220        230        240 
LALPYNNVAA VEQAFTKFKG QIACVIVEPI VGNMGCVPPA ADYLQALSDI TKREGAVLIV 

       250        260        270        280        290        300 
DEVMTGFRVA YGGAQELYGL KPDLVTLGKI IGGGLPVAAY GGRKDIMDKI APLGPVYQAG 

       310        320        330        340        350        360 
TLSGNPLAMA AGLAMLCHLR DNAMEIYPRL DQLSADLVNR VLDAAREAGV ALTANRVGSM 

       370        380        390        400        410        420 
FTWFFTDKHV TDWDSAATCD TKQFGQFHGA MLDAGVWLPP AQFEAAFLSS AHTEQDIDDT 

       430 
VAAAREAFAI L 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF43548.1.
RefSeqYP_593622.1. NC_008009.1.

3D structure databases

ProteinModelPortalQ1IHV2.
SMRQ1IHV2. Positions 6-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204669.Acid345_4548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF43548; ABF43548; Acid345_4548.
GeneID4071493.
KEGGaba:Acid345_4548.
PATRIC31986495. VBICanKor57425_4859.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMALMAHIAP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycKVER204669:GHL8-4595-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_KORVE
AccessionPrimary (citable) accession number: Q1IHV2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 62 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