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C1D9B6 (GSA_LARHH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 41. 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:LHK_00018
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeLaribacter

Protein attributes

Sequence length425 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 – 425425Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201024

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1D9B6 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 11B89C3F8AC68355

FASTA42544,962
        10         20         30         40         50         60 
MDRNQQLFER AKHVIPGGVN SPVRAFGSVG GSPRFIKRAQ GAYMWDADDR RLIDYIGSWG 

        70         80         90        100        110        120 
PMILGHAHPA VVEAVQQAAV HGLSFGTPTE AEIGIAEEIC KLMPSIERVR LVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGFT GRDAIIKFEG CYHGHSDSLL VKAGSGLLTF GNPSSAGVPE DFTRHTLVLE 

       190        200        210        220        230        240 
YNNVEQLERT FAEIGERIAC VILEPVAGNM NLIRPSAAFV QALRTLTQQH GSVLIYDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QSLHGIQPDL TTLGKVVGGG MPIGAFGGRA DIMNCIAPLG SVYQAGTLSG 

       310        320        330        340        350        360 
NPVAVAAGLA TLRLIQQPGF YDALAARTAR LVDGMVAAAR EAGIPFSGDC VGGMFGLYFA 

       370        380        390        400        410        420 
ADVPTSYAEV TASDRERFNA FFHAMLEAGV YLAPSAYEAG FVSAAHTDAD IDATVDAARQ 


AFARI 

« Hide

References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLHK9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001154 Genomic DNA. Translation: ACO73014.1.
RefSeqYP_002794024.1. NC_012559.1.

3D structure databases

ProteinModelPortalC1D9B6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557598.LHK_00018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO73014; ACO73014; LHK_00018.
GeneID7755648.
KEGGlhk:LHK_00018.
PATRIC22297167. VBILarHon49832_0019.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLHON557598:GHO5-19-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_LARHH
AccessionPrimary (citable) accession number: C1D9B6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 41 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