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C4LAK4 (GSA_TOLAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Tola_0579
OrganismTolumonas auensis (strain DSM 9187 / TA4) [Complete proteome] [HAMAP]
Taxonomic identifier595494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeTolumonas

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
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_0000382389

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C4LAK4 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: ABDFFCAD43534A12

FASTA43145,845
        10         20         30         40         50         60 
MAYSTQRSEQ LFTAAQQSIP GGVNSPVRAF NGVGGTPRFI AKADGAYLFD VDGNRYIDYV 

        70         80         90        100        110        120 
GSWGPMLLGH NHPAIKAAVL AAVENGLSYG APTESEVLMA EMIRQIMPDM EMVRMVNSGT 

       130        140        150        160        170        180 
EATMSAIRLA RGYTGRDKIV KFEGCYHGHA DCLLVKAGSG ALTLGQPNSP GVPADFAKHT 

       190        200        210        220        230        240 
LTCTYNDLAS VEATFASYGS EIACIIVEPV AGNMNCIPPV PGFLEGLRAI CDKYGALLII 

       250        260        270        280        290        300 
DEVMTGFRVS LQGAQGYYGI TPDLTTLGKI IGGGMPVGAF GGKKEIMAYI APTGPVYQAG 

       310        320        330        340        350        360 
TLSGNPVAMA AGLAMLKAIQ QPGLYDTLAE KTRQVAEGLK AAAAKQGIPL TVNYVGAMFG 

       370        380        390        400        410        420 
FFFTDEPEIT RFEQVSRCDI DAFRRFYHLM LQEGVYLAPS AYEAGFLSLA HSEADIAETL 

       430 
AAAERCFAQM K 

« Hide

References

[1]"Complete sequence of Tolumonas auensis DSM 9187."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S., Beller H.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9187 / TA4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001616 Genomic DNA. Translation: ACQ92208.1.
RefSeqYP_002891794.1. NC_012691.1.

3D structure databases

ProteinModelPortalC4LAK4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595494.Tola_0579.

Proteomic databases

PRIDEC4LAK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ92208; ACQ92208; Tola_0579.
GeneID7886444.
KEGGtau:Tola_0579.
PATRIC23977759. VBITolAue42623_0581.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTAUE595494:GHEF-603-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_TOLAT
AccessionPrimary (citable) accession number: C4LAK4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 36 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