DHA_BILW3
ID DHA_BILW3 Reviewed; 377 AA.
AC E5Y944;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:30718429};
DE EC=1.4.1.1 {ECO:0000250|UniProtKB:Q9AIK2};
GN Name=ald {ECO:0000303|PubMed:30718429};
GN ORFNames=HMPREF0179_02712 {ECO:0000312|EMBL:EFV43469.1};
OS Bilophila wadsworthia (strain 3_1_6).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Bilophila.
OX NCBI_TaxID=563192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_6;
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bilophila wadsworthia 3_1_6.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INDUCTION BY TAURINE, AND PATHWAY.
RC STRAIN=3_1_6;
RX PubMed=30718429; DOI=10.1073/pnas.1815661116;
RA Peck S.C., Denger K., Burrichter A., Irwin S.M., Balskus E.P.,
RA Schleheck D.;
RT "A glycyl radical enzyme enables hydrogen sulfide production by the human
RT intestinal bacterium Bilophila wadsworthia.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:3171-3176(2019).
CC -!- FUNCTION: Involved in an anaerobic respiration pathway that converts
CC the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and
CC sulfide. Acts as an alanine dehydrogenase that regenerates pyruvate,
CC the amino group acceptor for the taurine--pyruvate aminotransferase
CC enzyme, and liberates ammonia. {ECO:0000305|PubMed:30718429}.
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:0000250|UniProtKB:Q9AIK2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18406;
CC Evidence={ECO:0000250|UniProtKB:Q9AIK2};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000305|PubMed:30718429}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q9AIK2}.
CC -!- INDUCTION: Highly up-regulated in the presence of taurine.
CC {ECO:0000269|PubMed:30718429}.
CC -!- MISCELLANEOUS: Taurine is an abundant dietary and host-derived molecule
CC whose metabolism to hydrogen sulfide (H2S) by members of the human gut
CC microbiota has many prominent connections to host health and disease.
CC The human gut bacterium and opportunistic pathogen Bilophila
CC wadsworthia produces H2S when respiring sulfite (HSO3-) released from
CC organosulfonate substrates such as taurine and isethionate.
CC {ECO:0000305|PubMed:30718429}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADCP02000001; EFV43469.1; -; Genomic_DNA.
DR RefSeq; WP_005028751.1; NZ_KE150238.1.
DR AlphaFoldDB; E5Y944; -.
DR SMR; E5Y944; -.
DR STRING; 563192.HMPREF0179_02712; -.
DR EnsemblBacteria; EFV43469; EFV43469; HMPREF0179_02712.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_7; -.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000006034; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR CDD; cd05305; L-AlaDH; 1.
DR InterPro; IPR008141; Ala_DH.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
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; PS00837; ALADH_PNT_2; 1.
PE 2: Evidence at transcript level;
KW NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..377
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000450952"
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-1"
FT ACT_SITE 269
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-1"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-2"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-2"
FT BINDING 133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
FT BINDING 219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
FT BINDING 238..239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
FT BINDING 266..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
FT BINDING 304..307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000183-3"
SQ SEQUENCE 377 AA; 39853 MW; A1545C407984704D CRC64;
MRVGIPTEIK VQEFRVGITP AGVHALKEAG HTVLVQKGAG LGSMITDEEY VAAGAQMVAT
AKECWDCDMV VKVKEPLAPE YDLFHEGLIL YTYLHLAPEP ALTKALLEKK VIGIAYETVQ
FDNGFLPLLA PMSEVAGRMA TQVGAQMLTK IEGGMGLLMG GTAGVQAAHV VILGAGTVGL
SAAKVAMGMG ARVTILDSNL FRLRQIDDLF GGRIQTLASN AFNIAAATKD ADLLVGSVLI
PGALTPKLVT EAMVKTMKPG SAIVDVAIDQ GGCIEPTAKH GATYHDKPTF KYPVNGGEVV
CYSVGNMPGA VARTSTFTLT NATMPYMVDL ANKGWKKACQ DDKALARGIN TYDGKVYFKG
VSDALGYELH CTCDILK
