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A0RXB3 (GSA1_CENSY) 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 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:CENSYa_1357
OrganismCenarchaeum symbiosum (strain A) [Reference proteome] [HAMAP]
Taxonomic identifier414004 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaCenarchaealesCenarchaeaceaeCenarchaeum

Protein attributes

Sequence length421 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

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Sequence caution

The sequence ABK77980.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference 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 – 421421Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000382393

Amino acid modifications

Modified residue2581N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RXB3 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: BCE8564B16EC352D

FASTA42144,446
        10         20         30         40         50         60 
MGSRGLFERA RKVIPSGVNS PVRYYAPYPF FAASASGGSI RDADGRKYTD LCNGYGALLL 

        70         80         90        100        110        120 
GHGRGEVVRA VSAQLRRGTL FCVPTEQEVE LARLISGNYP SMESTRLVNT GGEATMTAIR 

       130        140        150        160        170        180 
LARGFTKRDR IIKFDGCYHG AHGSVLVKAG SGSAHLGIST SEGVPRGLAR QTTVIPYNDE 

       190        200        210        220        230        240 
AAFEGAAADD VAAVIVEPVM GNMGVIPPKK GFLRLLRKLS SRLGMQLIFD ETITGFRLSA 

       250        260        270        280        290        300 
GGAQEAFGVR PDITTLAKAL GGGLPIAAVG GKKNIMERLA PGGSVYEAST FAGNPVSVSA 

       310        320        330        340        350        360 
ALASIRTINR IKGRLYPRLE RAAAALASSI ADDAADLGLD RQINRVASIF QVFFTAEPVT 

       370        380        390        400        410        420 
DAASAKRADA ARFDKMFRAL LKNGVFVAPS QFEMASLSAA HTVEDLRNVS AAYRTALGAA 


R 

« Hide

References

[1]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DP000238 Genomic DNA. Translation: ABK77980.1. Different initiation.
RefSeqYP_876284.1. NC_014820.1.

3D structure databases

ProteinModelPortalA0RXB3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK77980; ABK77980; CENSYa_1357.
GeneID6371537.
KEGGcsy:CENSYa_1357.

Phylogenomic databases

HOGENOMHOG000020210.
KOK01845.

Enzyme and pathway databases

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]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGSA1_CENSY
AccessionPrimary (citable) accession number: A0RXB3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 43 of the entry and version 2 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