ID A0A161XP42_9EURY Unreviewed; 328 AA.
AC A0A161XP42;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Alanine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00935};
DE Short=AlaDH {ECO:0000256|HAMAP-Rule:MF_00935};
DE EC=1.4.1.1 {ECO:0000256|HAMAP-Rule:MF_00935};
GN Name=ala {ECO:0000256|HAMAP-Rule:MF_00935};
GN ORFNames=A4G99_00135 {ECO:0000313|EMBL:KZN24994.1};
OS Haladaptatus sp. R4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN24994.1, ECO:0000313|Proteomes:UP000076599};
RN [1] {ECO:0000313|EMBL:KZN24994.1, ECO:0000313|Proteomes:UP000076599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R4 {ECO:0000313|EMBL:KZN24994.1,
RC ECO:0000313|Proteomes:UP000076599};
RA Mukhopadhyay S.K.;
RT "Genome sequence of halophilic archaea.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidative deamination of L-
CC alanine to pyruvate, and the reverse reaction, the reductive amination
CC of pyruvate. {ECO:0000256|HAMAP-Rule:MF_00935}.
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|HAMAP-Rule:MF_00935};
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. Archaeal alanine dehydrogenase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00935}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00935}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN24994.1}.
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DR EMBL; LWHG01000011; KZN24994.1; -; Genomic_DNA.
DR RefSeq; WP_066139635.1; NZ_LWHG01000011.1.
DR AlphaFoldDB; A0A161XP42; -.
DR STRING; 1679489.A4G99_00135; -.
DR OrthoDB; 21421at2157; -.
DR Proteomes; UP000076599; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR HAMAP; MF_00935; AlaDH_arch; 1.
DR InterPro; IPR028609; AlaDH_arch-typ.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_00935};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00935};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00935}.
FT ACT_SITE 71
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 142..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 223..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ SEQUENCE 328 AA; 35105 MW; FF026E18A1D8F78E CRC64;
METLLLNQDA VDENTQMPEL IRAIEDAFAA YALGDAQMPA KSYIDLPQYN GDFRSMPAYL
DADGWDAAGI KWVNVHPDNP DGFDLPTVMG TMIYSDPETA YPLAIMDGTE LTMKRTGAAA
AVATDYLAVE DATSMGLVGA GVQSYTQLEA ISKIRPIEEV VISDLDEEAV ADFIDYFDDE
FDVRAGSISE AASCDILSTV TPVESPIVSA DAVGEHTHIN AMGADAEGKH EIADEVLLNA
KLVIDDHAQT THSGEINVPY NEGTLADDDI HGDIGDIVIG DLEGRTEDDG VTVFDSTGLA
IQDVAAAHVV YEHANENDNG YPFDLLGV
//
