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Q72K83 (GSA_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:TT_C0564
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243635

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72K83 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 863056906C1FB22B

FASTA42746,379
        10         20         30         40         50         60 
MEGMERPISE AYFQEAKRHI PGGVSSPVRA FKAVGGTPPF LVRGEGAYVW DADGNRYLDY 

        70         80         90        100        110        120 
VMSWGPLILG HAHPKVLARV RETLERGLTF GAPSPLEVAL AKKVKRAYPF VDLVRFVNSG 

       130        140        150        160        170        180 
TEATMSALRL ARGYTNRPYI VKFRGNYHGH ADGLLVEAGS GALTLGVPSS AGVPEEYAKL 

       190        200        210        220        230        240 
TLVLEYNDPE GLREVLRRRG EEIAAIIFEP VVGNAGVLVP TEDFLKALHE AREFGVLLIA 

       250        260        270        280        290        300 
DEVMTGFRLA FGGATELLGL KPDLVTLGKV LGGGLPAAAY AGRREIMEKV APLGPVYQAG 

       310        320        330        340        350        360 
TLSGNPLAMA AGLATLELLE ENPGYYRYLE DLGARLERGL KEVLAQKGIP HAVNRVGSMV 

       370        380        390        400        410        420 
TVFFTEGPVV TFQDAKRTDT ELFKRFFHGL LDRGIYWPPS NFEAAFLSVA HTEEDVEKTL 


EALGEAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017221 Genomic DNA. Translation: AAS80912.1.
RefSeqYP_004539.1. NC_005835.1.

3D structure databases

ProteinModelPortalQ72K83.
SMRQ72K83. Positions 4-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC0564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS80912; AAS80912; TT_C0564.
GeneID2775165.
KEGGtth:TTC0564.
PATRIC23951535. VBITheThe54392_0563.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMAKRLMEPG.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycTTHE262724:GCAT-577-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_THET2
AccessionPrimary (citable) accession number: Q72K83
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 71 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