ID D1B5S2_THEAS Unreviewed; 370 AA.
AC D1B5S2;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
GN OrderedLocusNames=Taci_1131 {ECO:0000313|EMBL:ACZ19363.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19363.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ19363.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
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:0000256|PIRNR:PIRNR000183};
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
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DR EMBL; CP001818; ACZ19363.1; -; Genomic_DNA.
DR RefSeq; WP_012869878.1; NC_013522.1.
DR RefSeq; YP_003317645.1; NC_013522.1.
DR AlphaFoldDB; D1B5S2; -.
DR STRING; 525903.Taci_1131; -.
DR EnsemblBacteria; ACZ19363; ACZ19363; Taci_1131.
DR KEGG; tai:Taci_1131; -.
DR PATRIC; fig|525903.6.peg.1130; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_0; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000002030; Chromosome.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR CDD; cd05305; L-AlaDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 NCBIfam; TIGR00518; alaDH; 1.
DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE 1; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000183};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000183};
KW Reference proteome {ECO:0000313|Proteomes:UP000002030}.
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..297
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT ACT_SITE 96
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT ACT_SITE 270
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 239..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 267..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 298..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ SEQUENCE 370 AA; 39729 MW; E5AFF92F07AC2549 CRC64;
MKIGCPKEIK NHEYRVGLIP ASVRTYVASG HEVFVQKGAG LGSGIADEEY VAAGAKILDT
AEEVWAKADM IVKVKEPLPQ EYPLMREGQL LYTYFHFAAS EELTKACMER KIVALAYETV
EDQDGSLPLL KPMSEVAGRM APLMGSFYLG KAHGGRGLLV SGVPGVAPCN VLVLGGGVVG
RNAARMAAGL GAKVTILDVK AKVLEYLDDT MPSNVFPVYS DPVTLEENLK EADMVIGAVL
IPGAKAPKLV RKEHLKIMKP GAVMVDVAID QGGCFETSHA TTHSDPIYVV DGIVHYCVAN
MPGAYARTST FALNNATIYY GKMLADKGYI QACKDNPGLK KGLNMVMGKV TYKPVAEAFD
LPYTPVDEVL
//
