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B5ERN9 (GSA_ACIF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Lferr_2901
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121852

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B5ERN9 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 5D79E349A3FECCB9

FASTA43045,193
        10         20         30         40         50         60 
MTQTSHALFH MAQQCIPGGV NSPVRAFRGV GGDPIFIDHA EGPFFWDVEG KRYLDYVGSW 

        70         80         90        100        110        120 
GPMIHGHGHP EVLAAVHAQV NKGLGFGAPT AIEVEMAELV CALVPGIESV RMTSSGTEAV 

       130        140        150        160        170        180 
MTAIRLARGY TGRDRIIKFE GNYHGHSDSL LVKAGSGALT LGQPSSAGVP REVSQNTLVL 

       190        200        210        220        230        240 
PYNDLPAVVE MMAQFGFDVA TIIVEPVAGN MGCVPPEPGF LEGLRAVCDQ YGCVLIFDEV 

       250        260        270        280        290        300 
MTGFRVALGG AQALYGVRPD LTTLGKIIGG GLPVGAVGGP REIMEYLAPT GPVYQAGTLS 

       310        320        330        340        350        360 
GNPVAMAAGL ATLRLLTVPG FHERLAAQTA VLCEGLAERA EAAGVPMQIN HVPGMFGWFF 

       370        380        390        400        410        420 
AEQPVRGFDT VMAADSKRYA RFFHGLLARG VYLAPSAYEA GFLSAAHGDT EIAATLDAAE 

       430 
AVLATLKEDA 

« Hide

References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53993.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001132 Genomic DNA. Translation: ACH85085.1.
RefSeqYP_002221292.1. NC_011206.1.

3D structure databases

ProteinModelPortalB5ERN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380394.Lferr_2901.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH85085; ACH85085; Lferr_2901.
GeneID6878905.
KEGGafe:Lferr_2901.
PATRIC20663388. VBIAciFer6930_2869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAFER380394:GHE0-2956-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_ACIF5
AccessionPrimary (citable) accession number: B5ERN9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 14, 2008
Last modified: February 19, 2014
This is version 43 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