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C4L367 (GSA1_EXISA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:EAT1b_2420
OrganismExiguobacterium sp. (strain ATCC BAA-1283 / AT1b) [Complete proteome] [HAMAP]
Taxonomic identifier360911 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length432 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000382315

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C4L367 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: A1F48ECC8D9C85E1

FASTA43246,541
        10         20         30         40         50         60 
MTTSSNRQSS DALYQDALTH IVGGVNSPSR SFKAVGGGAP VYMERGEGAY FYDVDGNRYI 

        70         80         90        100        110        120 
DYLAAYGPII TGHAHPHIHE ALMNASSKGL LYGTPHRLEV EFAKKLKQAI PSMDKVRFTN 

       130        140        150        160        170        180 
SGTEAVMTTV RVARAYTGRE LVVKFSGCYH GHSDLMLIAA GSGPATLGSP DSAGVTKATA 

       190        200        210        220        230        240 
KEVITVPFND VEAYREMMKE WGDQVACVLV EPIVGNFGIV EPKPGFLQAV NDITHEHGAL 

       250        260        270        280        290        300 
VIYDEVITAF RFTYGSAQQV YGIEPDMTAL GKIIGGGLPI GAYGGKAEIM ETVAPLGPAY 

       310        320        330        340        350        360 
QAGTMAGNPA SMATGIACLE VLEQPGVYEK LDALGAKLEA GIREAAEKHD VTITLNRLKG 

       370        380        390        400        410        420 
ALTVYFTDEI VTDYEGAEKS DGEKFGRFFK LMLENGVNLA PSKYEAWFLT TEHTEQDIEE 

       430 
TIEAVNRSFA QL 

« Hide

References

[1]"Complete sequence of Exiguobacterium sp. AT1b."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G. expand/collapse author list , Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., Kathariou S., Tiedje J.M., Richardson P.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1283 / AT1b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001615 Genomic DNA. Translation: ACQ71341.1.
RefSeqYP_002886786.1. NC_012673.1.

3D structure databases

ProteinModelPortalC4L367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360911.EAT1b_2420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ71341; ACQ71341; EAT1b_2420.
GeneID7869977.
KEGGeat:EAT1b_2420.
PATRIC21880078. VBIExiSp39724_2403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAITINRLK.
OrthoDBEOG6QVRHN.
ProtClustDBPRK12389.

Enzyme and pathway databases

BioCycESP360911:GI4R-2499-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.
ProtoNetSearch...

Entry information

Entry nameGSA1_EXISA
AccessionPrimary (citable) accession number: C4L367
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 38 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