DHA_BACSU
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 03-AUG-2022, entry version 141.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:6794611};
DE EC=1.4.1.1 {ECO:0000269|PubMed:6794611};
DE AltName: Full=Stage V sporulation protein N {ECO:0000303|PubMed:8226620};
GN Name=ald {ECO:0000303|PubMed:8226620};
GN Synonyms=ski22 {ECO:0000303|PubMed:8226620},
GN spoVN {ECO:0000303|PubMed:8226620}; OrderedLocusNames=BSU31930;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, FUNCTION IN SPORULATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=8226620; DOI=10.1128/jb.175.21.6789-6796.1993;
RA Siranosian K.J., Ireton K., Grossman A.D.;
RT "Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus
RT 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 degrees of
RT 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 PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC MECHANISM.
RX PubMed=6794611; DOI=10.1021/bi00523a002;
RA Grimshaw C.E., Cleland W.W.;
RT "Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase.";
RL Biochemistry 20:5650-5655(1981).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=6794612; DOI=10.1021/bi00523a003;
RA Grimshaw C.E., Cook P.F., Cleland W.W.;
RT "Use of isotope effects and pH studies to determine the chemical mechanism
RT of Bacillus subtilis L-alanine dehydrogenase.";
RL Biochemistry 20:5655-5661(1981).
RN [6]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=22797752; DOI=10.1128/jb.00778-12;
RA Lin T.H., Wei G.T., Su C.C., Shaw G.C.;
RT "AdeR, a PucR-type transcription factor, activates expression of L-alanine
RT dehydrogenase and is required for sporulation of Bacillus subtilis.";
RL J. Bacteriol. 194:4995-5001(2012).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of L-alanine
CC to pyruvate. Oxidative deamination proceeds through a sequential,
CC ordered ternary-binary mechanism, where NAD(+) binds first followed by
CC L-alanine; the products are released in the order ammonia, pyruvate and
CC NADH (PubMed:6794611, PubMed:6794612) (Probable). Disruption blocks
CC sporulation probably in stage V; 20-30% sporulation can be restored if
CC the media is supplemented with pyruvate, suggesting lack of pyruvate
CC blocks sporulation. Thus it is a key factor in the assimilation of L-
CC alanine as an energy source via the tricarboxylic acid cycle during
CC sporulation (PubMed:8226620). {ECO:0000269|PubMed:6794611,
CC ECO:0000269|PubMed:6794612, ECO:0000269|PubMed:8226620,
CC ECO:0000305|PubMed:8226620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1;
CC Evidence={ECO:0000269|PubMed:6794611, ECO:0000269|PubMed:6794612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18406;
CC Evidence={ECO:0000269|PubMed:6794611, ECO:0000269|PubMed:6794612};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18407;
CC Evidence={ECO:0000269|PubMed:6794611, ECO:0000269|PubMed:6794612};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homohexamer. Trimer of dimer (By similarity).
CC {ECO:0000250|UniProtKB:P9WQB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0QVQ8}.
CC -!- INDUCTION: A monocistronic operon. Induced by L-alanine in minimal
CC media. Constitutively expressed in rich medium, declines during
CC sporulation. Induced early during sporulation on minimal medium by L-
CC alanine. Affects its own expression (PubMed:8226620). Transcription
CC activated by AdeR (PubMed:22797752). {ECO:0000269|PubMed:22797752,
CC ECO:0000269|PubMed:8226620}.
CC -!- DISRUPTION PHENOTYPE: Strain cannot grow on L-alanine as a sole carbon
CC source. Disruption of ald causes a sporulation defect, most likely in
CC stage V. {ECO:0000269|PubMed:8226620}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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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; NC_000964.3.
DR RefSeq; WP_003243280.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; Q08352; -.
DR SMR; Q08352; -.
DR STRING; 224308.BSU31930; -.
DR jPOST; Q08352; -.
DR PaxDb; Q08352; -.
DR PRIDE; Q08352; -.
DR EnsemblBacteria; CAB15181; CAB15181; BSU_31930.
DR GeneID; 936557; -.
DR KEGG; bsu:BSU31930; -.
DR PATRIC; fig|224308.179.peg.3459; -.
DR eggNOG; COG0686; Bacteria.
DR InParanoid; Q08352; -.
DR OMA; HITTHDQ; -.
DR PhylomeDB; Q08352; -.
DR BioCyc; BSUB:BSU31930-MON; -.
DR BioCyc; MetaCyc:MON-12812; -.
DR BRENDA; 1.4.1.1; 658.
DR SABIO-RK; Q08352; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006524; P:alanine catabolic process; ISS:UniProtKB.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:UniProtKB.
DR CDD; cd05305; L-AlaDH; 1.
DR InterPro; IPR008141; Ala_DH.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42795; PTHR42795; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR PIRSF; PIRSF000183; Alanine_dh; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00518; alaDH; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome;
KW Sporulation.
FT CHAIN 1..378
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000198992"
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 176..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 265..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 297..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
