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Q08352 (DHA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine dehydrogenase
EC=1.4.1.1
Alternative name(s):
Stage V sporulation protein N
Gene names
Name:ald
Synonyms:spoVN
Ordered Locus Names:BSU31930
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme is a key factor in the assimilation of L-alanine as an energy source through the tricarboxylic acid cycle during sporulation.

Catalytic activity

L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH.

Pathway

Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the AlaDH/PNT family.

Ontologies

Keywords
   Biological processSporulation
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processsporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalanine dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Alanine dehydrogenase
PRO_0000198992

Regions

Nucleotide binding168 – 19831NAD By similarity

Sites

Active site951 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08352 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: B5D6113047FCF211

FASTA37839,684
        10         20         30         40         50         60 
MIIGVPKEIK NNENRVALTP GGVSQLISNG HRVLVETGAG LGSGFENEAY ESAGAEIIAD 

        70         80         90        100        110        120 
PKQVWDAEMV MKVKEPLPEE YVYFRKGLVL FTYLHLAAEP ELAQALKDKG VTAIAYETVS 

       130        140        150        160        170        180 
EGRTLPLLTP MSEVAGRMAA QIGAQFLEKP KGGKGILLAG VPGVSRGKVT IIGGGVVGTN 

       190        200        210        220        230        240 
AAKMAVGLGA DVTIIDLNAD RLRQLDDIFG HQIKTLISNP VNIADAVAEA DLLICAVLIP 

       250        260        270        280        290        300 
GAKAPTLVTE EMVKQMKPGS VIVDVAIDQG GIVETVDHIT THDQPTYEKH GVVHYAVANM 

       310        320        330        340        350        360 
PGAVPRTSTI ALTNVTVPYA LQIANKGAVK ALADNTALRA GLNTANGHVT YEAVARDLGY 

       370 
EYVPAEKALQ DESSVAGA

« Hide

References

« Hide 'large scale' references
[1]"Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus subtilis."
Siranosian K.J., Ireton K., Grossman A.D.
J. Bacteriol. 175:6789-6796(1993) [PubMed: 8226620] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Sequence of a DNA fragment of 12315 bp around ald at about 253 degrees of the genome of Bacillus subtilis."
Oudega B., Vandenbol M., Koningstein G.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L20916 Genomic DNA. Translation: AAA16038.1.
Z82015 Genomic DNA. Translation: CAB04775.1.
AL009126 Genomic DNA. Translation: CAB15181.1.
PIRA49337.
RefSeqNP_391071.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ08352.
SMRQ08352. Positions 1-358.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003424; EBBACP00000003424; EBBACG00000003417.
GeneID936557.
GenomeReviewsGene locus BSU31930 in contig AL009126_GR.
KEGGbsu:BSU31930.
NMPDRfig|224308.1.peg.3196.
PATRIC18978358. VBIBacSub10457_3342.

Organism-specific databases

GenoListBSU31930. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000823.
HOGENOMHBG289735.
OMAMNIAEAV.
PhylomeDBQ08352.
ProtClustDBCLSK887816.

Enzyme and pathway databases

BioCycBSUB:BSU31930-MONOMER.
MetaCyc:MONOMER-12812.

Family and domain databases

InterProIPR008142. Ala_DH/PNT_CS1.
IPR008143. Ala_DH/PNT_CS2.
IPR008141. Ala_DH/Pyr_transHydgase.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
[Graphical view]
KOK00259.
PANTHERPTHR10160:SF3. PTHR10160:SF3. 1 hit.
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
PIRSFPIRSF000183. Alanine_dh. 1 hit.
SMARTSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00518. AlaDH. 1 hit.
PROSITEPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHA_BACSU
AccessionPrimary (citable) accession number: Q08352
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 25, 2012
This is version 89 of the entry and version 1 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

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