ID DHA_BACSU Reviewed; 378 AA. AC Q08352; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 16-JUN-2009, entry version 67. DE RecName: Full=Alanine dehydrogenase; DE EC=1.4.1.1; DE AltName: Full=Stage V sporulation protein N; GN Name=ald; Synonyms=spoVN; OrderedLocusNames=BSU31930; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=94042840; PubMed=8226620; RA Siranosian K.J., Ireton K., Grossman A.D.; RT "Alanine dehydrogenase (ald) is required for normal sporulation in RT Bacillus subtilis."; RL J. Bacteriol. 175:6789-6796(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Oudega B., Vandenbol M., Koningstein G.; RT "Sequence of a DNA fragment of 12315 bp around ald at about 253 RT degrees of the genome of Bacillus subtilis."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- FUNCTION: This enzyme is a key factor in the assimilation of L- CC alanine as an energy source through the tricarboxylic acid cycle CC during sporulation. CC -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) CC + NADH. CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step CC 1/1. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L20916; AAA16038.1; -; Genomic_DNA. DR EMBL; Z82015; CAB04775.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15181.1; -; Genomic_DNA. DR PIR; A49337; A49337. DR RefSeq; NP_391071.1; -. DR HSSP; O52942; 1SAY. DR GeneID; 936557; -. DR GenomeReviews; AL009126_GR; BSU31930. DR KEGG; bsu:BSU31930; -. DR NMPDR; fig|224308.1.peg.3196; -. DR SubtiList; BG10468; ald. DR HOGENOM; Q08352; -. DR OMA; Q08352; MGARVTI. DR BioCyc; BSUB224308:BSU3188-MON; -. DR BioCyc; MetaCyc:MON-12812; -. DR BRENDA; 1.4.1.1; 150. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:EC. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0030435; P:sporulation resulting in formation of a cel...; IEA:UniProtKB-KW. DR InterPro; IPR007698; Ala_DH/PNT_C. DR InterPro; IPR008142; Ala_DH/PNT_CS1. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR007886; Ala_DH/PNT_N. DR InterPro; IPR008141; Ala_DH_PNT. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR00518; alaDH; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Sporulation. FT CHAIN 1 378 Alanine dehydrogenase. FT /FTId=PRO_0000198992. FT NP_BIND 168 198 NAD (By similarity). FT ACT_SITE 95 95 By similarity. SQ SEQUENCE 378 AA; 39684 MW; B5D6113047FCF211 CRC64; MIIGVPKEIK NNENRVALTP GGVSQLISNG HRVLVETGAG LGSGFENEAY ESAGAEIIAD PKQVWDAEMV MKVKEPLPEE YVYFRKGLVL FTYLHLAAEP ELAQALKDKG VTAIAYETVS EGRTLPLLTP MSEVAGRMAA QIGAQFLEKP KGGKGILLAG VPGVSRGKVT IIGGGVVGTN AAKMAVGLGA DVTIIDLNAD RLRQLDDIFG HQIKTLISNP VNIADAVAEA DLLICAVLIP GAKAPTLVTE EMVKQMKPGS VIVDVAIDQG GIVETVDHIT THDQPTYEKH GVVHYAVANM PGAVPRTSTI ALTNVTVPYA LQIANKGAVK ALADNTALRA GLNTANGHVT YEAVARDLGY EYVPAEKALQ DESSVAGA //