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A4IKL1 (GSA1_GEOTN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Ordered Locus Names:GTNG_0483
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length428 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000382319

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IKL1 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 5E210EF04C10D286

FASTA42846,206
        10         20         30         40         50         60 
MQWTKSEQLY EEALRHIVGG VNSPSRSYKA VGGGAPVVME RAQGAYFWDV DGNKYIDYLA 

        70         80         90        100        110        120 
AYGPIITGHA HPHITAAIQR AAETGVLYGT PTPHEITFAK MLKEAIPSLE KVRFVNSGTE 

       130        140        150        160        170        180 
AVMTTIRVAR AYTGRSKIVK FAGCYHGHSD LVLVAAGSGP STLGTPDSAG VPQSIAHEVI 

       190        200        210        220        230        240 
TVPYNDVESF REAMNVWGEH VAAVLVEPIV GNFGIVLPKP GFLEAVNDIA HEAGALVIYD 

       250        260        270        280        290        300 
EVITAFRFMY GGAQNLLGIE PDMTAMGKII GGGLPIGAYG GRQDIMEQVA PLGPAYQAGT 

       310        320        330        340        350        360 
MAGNPASMLA GIACLEVLKQ EGVYEHLDRL GAMLEEGIMT HARQCGLPVT INRLKGALTV 

       370        380        390        400        410        420 
FFTEEKVENY EQAQRSDGEL FAKFFKLMLK QGVNLAPSKY EAWFITLAHT EDDIAYTIDA 


VGRAFRQL 

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References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NG80-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000557 Genomic DNA. Translation: ABO65865.1.
RefSeqYP_001124610.1. NC_009328.1.

3D structure databases

ProteinModelPortalA4IKL1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420246.GTNG_0483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO65865; ABO65865; GTNG_0483.
GeneID4965427.
KEGGgtn:GTNG_0483.
PATRIC21977187. VBIGeoThe136879_0502.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAFNDIDSY.
OrthoDBEOG6QVRHN.
ProtClustDBPRK12389.

Enzyme and pathway databases

BioCycGTHE420246:GIXT-531-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 nameGSA1_GEOTN
AccessionPrimary (citable) accession number: A4IKL1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 1, 2007
Last modified: February 19, 2014
This is version 60 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