Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5I1Y2 (A5I1Y2_CLOBH) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Aspartate--ammonia ligase HAMAP MF_00555
EC=6.3.1.1 HAMAP MF_00555
Alternative name(s):
Asparagine synthetase A HAMAP MF_00555
Gene names
Name:asnA HAMAP MF_00555 EMBL CAL83046.1
Ordered Locus Names:CBO1504, CLC_1538
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine. SAAS SAAS004618 HAMAP MF_00555

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. SAAS SAAS004618 HAMAP MF_00555

Subcellular location

Cytoplasm By similarity SAAS SAAS004618 HAMAP MF_00555.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily. HAMAP MF_00555

Sequences

Sequence LengthMass (Da)Tools
A5I1Y2 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 43EDFD7054C63AB4

FASTA34039,537
        10         20         30         40         50         60 
MIKFKDRLMI PEGYESTLGI RETEVAIKKV KDFFERTLAE KLNLTRVSAP LFVRKNTGMN 

        70         80         90        100        110        120 
DNLNGVERPV DFDMKDLQDE MIEIVHSLAK WKRMALHRYD FKVGEGLYTD MNAIRRDEDL 

       130        140        150        160        170        180 
DNLHSIYVDQ WDWEKVIKKE DRNKETLKAI VNKIYSAFKE TERYICSQYE GFNEILPEKI 

       190        200        210        220        230        240 
CFITSQELQD TYPDLDSKER EDAITKEKGA VFLMEIGGVL ASGEKHDGRA PDYDDWTLNG 

       250        260        270        280        290        300 
DILFWNPVLE RAFELSSMGI RVDEESLEKQ LKIAGCEDRK KLEFHKLLLE GKLPYTVGGG 

       310        320        330        340 
IGQSRICMYF LRKAHIGEVQ ASIWPDLMIE DCEKVKINLL

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger].
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A [Los Alamos].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000727 Genomic DNA. Translation: ABS39038.1.
AM412317 Genomic DNA. Translation: CAL83046.1.
RefSeqYP_001254016.1. NC_009495.1.
YP_001387402.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5I1Y2.
SMRA5I1Y2. Positions 21-335.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5I1Y2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5187341.
5401417.
GenomeReviewsGene locus CBO1504 in contig AM412317_GR.
Gene locus CLC_1538 in contig CP000727_GR.
KEGGcbh:CLC_1538.
cbo:CBO1504.
PATRIC19365075. VBICloBot22612_1481.

Phylogenomic databases

eggNOGCOG2502.
HOGENOMHBG288146.
OMALNDNLNG.
ProtClustDBPRK05425.

Family and domain databases

HAMAPMF_00555. AsnA.
[Tree]
InterProIPR006195. aa-tRNA-synth_II.
IPR004618. AsnA.
[Graphical view]
KOK01914.
PfamPF03590. AsnA. 1 hit.
[Graphical view]
PIRSFPIRSF001555. Asp_ammon_ligase. 1 hit.
TIGRFAMsTIGR00669. AsnA. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA5I1Y2_CLOBH
AccessionPrimary (citable) accession number: A5I1Y2
Secondary accession number(s): A7G3N7
Entry history
Integrated into UniProtKB/TrEMBL: June 26, 2007
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info