ID D5UM81_TSUPD Unreviewed; 371 AA.
AC D5UM81;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=Tpau_1743 {ECO:0000313|EMBL:ADG78361.1};
OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP
OS 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
OS (Corynebacterium paurometabolum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG78361.1, ECO:0000313|Proteomes:UP000001213};
RN [1] {ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG78361.1, ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RX PubMed=21886861;
RA Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Tapia R.,
RA Han C., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA Yasawong M., Brambilla E.M., Rohde M., Sikorski J., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Tsukamurella paurometabola type strain (no.
RT 33).";
RL Stand. Genomic Sci. 4:342-351(2011).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine. {ECO:0000256|PIRNR:PIRNR000183}.
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 -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005206, 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; CP001966; ADG78361.1; -; Genomic_DNA.
DR RefSeq; WP_013126389.1; NC_014158.1.
DR AlphaFoldDB; D5UM81; -.
DR STRING; 521096.Tpau_1743; -.
DR KEGG; tpr:Tpau_1743; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_11; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000001213; 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:UniProtKB-UniPathway.
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; 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 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; PS00836; ALADH_PNT_1; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000183, ECO:0000256|PIRSR:PIRSR000183-3};
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:UP000001213}.
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 203
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 279
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 371 AA; 38168 MW; BF78C38F9F2608DD CRC64;
MRVGIPTEIK NNEYRVAITP GGVAELAKHG HDVLIEDGAG TGSAISNDDF AAAGARIVPS
ADDVWGEADL LLKVKEPIAP EYARMRADQT IFTYLHLAAS RPCTDALLAS KTTSIAYETV
QLADGSLPLL APMSEVAGRL APQVGSYHLM RSKGGRGVLM GGVPGTAPAK VTVLGGGVSG
INAAQIAAGM GADVTVFDLD VRKMRAVNAQ FGGRVHTSYS TSLALEEAVV ESDLVIGAVL
IPGAAAPKLV STDLVHRMRP GAVLVDIAID QGGCFADSRP TTHDDPTFTV GETVFYCVAN
MPGAVPRTST FALTGATLPY VLRIADKGWR GACTDDPALA AGLSTHDGEL LNASVGDALG
IAAKSPESVL G
//
