DHA_BILWA
ID DHA_BILWA Reviewed; 377 AA.
AC Q9AIK2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:11041346};
DE EC=1.4.1.1 {ECO:0000269|PubMed:11041346};
GN Name=ald {ECO:0000303|PubMed:11041346};
OS Bilophila wadsworthia.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Bilophila.
OX NCBI_TaxID=35833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP INDUCTION, SUBUNIT, AND PATHWAY.
RC STRAIN=DSM 11045 / RZATAU;
RX PubMed=11041346; DOI=10.1007/s002030000190;
RA Laue H., Cook A.M.;
RT "Purification, properties and primary structure of alanine dehydrogenase
RT involved in taurine metabolism in the anaerobe Bilophila wadsworthia.";
RL Arch. Microbiol. 174:162-167(2000).
CC -!- FUNCTION: Involved in an anaerobic respiration pathway that converts
CC the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and
CC sulfide. Catalyzes the oxidative deamination of alanine which
CC regenerates pyruvate, the amino group acceptor for the taurine--
CC pyruvate aminotransferase enzyme, and liberates ammonia. Can also
CC catalyze the reverse reaction in vitro. Cannot use NADP(H)(+) as a
CC substrate. To a lesser extent, is also able to deaminate L-2-
CC aminobutyrate in vitro, and in the amination reaction the enzyme can
CC utilize oxaloacetate and 2-oxobutyrate in addition to pyruvate.
CC {ECO:0000269|PubMed:11041346}.
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:11041346};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18406;
CC Evidence={ECO:0000305|PubMed:11041346};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for L-alanine (at pH 10 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:11041346};
CC KM=0.15 mM for NAD(+) (at pH 10 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:11041346};
CC KM=1.1 mM for pyruvate (at pH 9 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:11041346};
CC KM=31 mM for ammonia (at pH 9 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:11041346};
CC KM=0.04 mM for NADH (at pH 9 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:11041346};
CC Vmax=17 umol/sec/mg enzyme for the reductive amination of pyruvate
CC {ECO:0000269|PubMed:11041346};
CC Vmax=1.2 umol/sec/mg enzyme for the oxidative deamination of alanine
CC {ECO:0000269|PubMed:11041346};
CC pH dependence:
CC Optimum pH is 9.0 for reductive amination of pyruvate and pH 9.0-11.5
CC for oxidative deamination of alanine. {ECO:0000269|PubMed:11041346};
CC Temperature dependence:
CC Optimum temperature is 55-60 degrees Celsius for reductive amination
CC and 50-55 degrees Celsius for oxidative deamination. But at 60
CC degrees Celsius an inactivation of the enzyme is observed after about
CC 1 minute, while at 65 degrees Celsius the enzyme is inactive after
CC about 10 seconds. {ECO:0000269|PubMed:11041346};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000305|PubMed:11041346}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11041346}.
CC -!- INDUCTION: Up-regulated in the presence of taurine.
CC {ECO:0000269|PubMed:11041346}.
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}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; AF269148; AAK38118.1; -; Genomic_DNA.
DR RefSeq; WP_005028751.1; NZ_CABKPK010000001.1.
DR AlphaFoldDB; Q9AIK2; -.
DR SMR; Q9AIK2; -.
DR BioCyc; MetaCyc:MON-12510; -.
DR BRENDA; 1.4.1.1; 856.
DR UniPathway; UPA00338; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..377
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000450951"
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
