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P39909 (BLTD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spermine/spermidine acetyltransferase
EC=2.3.1.57
Gene names
Name:bltD
Synonyms:bmr2D, bmtD
Ordered Locus Names:BSU26600
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate. Ref.4

Catalytic activity

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.

Pathway

Amine and polyamine degradation; putrescine degradation; N-acetylputrescine from putrescine: step 1/1.

Sequence similarities

Contains 1 N-acetyltransferase domain.

Biophysicochemical properties

Kinetic parameters:

KM=67 µM for spermine Ref.4

KM=1200 µM for N 1-Acetylspermine

KM=200 µM for spermidine

Vmax=19.5 nmol/min/mg enzyme with spermine as substrate

Vmax=7.4 nmol/min/mg enzyme with N 1-Acetylspermine as substrate

Vmax=0.6 nmol/min/mg enzyme with spermidine as substrate

Ontologies

Keywords
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processputrescine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondiamine N-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Spermine/spermidine acetyltransferase
PRO_0000064945

Regions

Domain3 – 152150N-acetyltransferase

Experimental info

Sequence conflict851D → I in AAC36945. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39909 [UniParc].

Last modified August 4, 2003. Version 2.
Checksum: 4E6F7ACB3429DAE9

FASTA15217,838
        10         20         30         40         50         60 
MSINIKAVTD DNRAAILDLH VSQNQLSYIE STKVCLEDAK ECHYYKPVGL YYEGDLVGFA 

        70         80         90        100        110        120 
MYGLFPEYDE DNKNGRVWLD RFFIDERYQG KGLGKKMLKA LIQHLAELYK CKRIYLSIFE 

       130        140        150 
NNIHAIRLYQ RFGFQFNGEL DFNGEKVMVK EL

« Hide

References

« Hide 'large scale' references
[1]"Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated."
Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A.
J. Bacteriol. 177:3904-3910(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / BD170.
[2]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis."
Woolridge D.P., Martinez J.D., Stringer D.E., Gerner E.W.
Biochem. J. 340:753-758(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L32599 Genomic DNA. Translation: AAC36945.1.
D84432 Genomic DNA. Translation: BAA12354.1.
AL009126 Genomic DNA. Translation: CAB14601.1.
PIRB69595.
RefSeqNP_390537.1. NC_000964.3.

3D structure databases

ProteinModelPortalP39909.
SMRP39909. Positions 1-150.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU26600.

Proteomic databases

PaxDbP39909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14601; CAB14601; BSU26600.
GeneID937632.
KEGGbsu:BSU26600.
PATRIC18977162. VBIBacSub10457_2770.

Organism-specific databases

GenoListBSU26600. [Micado]

Phylogenomic databases

eggNOGCOG0454.
HOGENOMHOG000067992.
KOK00657.
OMAHICEVTA.
ProtClustDBCLSK887632.

Enzyme and pathway databases

BioCycBSUB:BSU26600-MONOMER.
UniPathwayUPA00188; UER00363.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLTD_BACSU
AccessionPrimary (citable) accession number: P39909
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: August 4, 2003
Last modified: May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents