ID M0AM67_NATA1 Unreviewed; 350 AA.
AC M0AM67;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=C481_17627 {ECO:0000313|EMBL:ELY98473.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELY98473.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELY98473.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELY98473.1,
RC ECO:0000313|Proteomes:UP000011554};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY98473.1}.
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DR EMBL; AOIO01000039; ELY98473.1; -; Genomic_DNA.
DR RefSeq; WP_006110630.1; NZ_AOIO01000039.1.
DR AlphaFoldDB; M0AM67; -.
DR STRING; 29540.C481_17627; -.
DR PATRIC; fig|29540.5.peg.3591; -.
DR eggNOG; arCOG01035; Archaea.
DR OMA; AVKAFTY; -.
DR OrthoDB; 21421at2157; -.
DR Proteomes; UP000011554; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 161..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 242..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ SEQUENCE 350 AA; 37255 MW; 49D68B15592AD4B7 CRC64;
MNTILLDSDD VDENIRMGAL IDAVEQAFGA FERGDTQMPA KSYIDLPQYN GDFRSMPAYL
NVRGSDASSS QSGSRRDADA ADGWDAAGLK WVNVHPDNPT DHDLPTVLGT MIYSDPETAF
PLAIMDGTTL TMKRTGAAAA VATDHLAVSD ATSLGLVGAG VQSYTQLDAI SEIRPIEEVV
VSDLDEERVQ RFIDAYDDEF TVRAGSISEA GHCDVLSTVT PVRDPVVTPE DVGEHTHINA
IGADAEGKHE LADELLQAAT VVIDDHEQCT HSGEINVPYT DGTLTDADIH AELGELVVGT
TDGRTAETDV TVFDSTGLAI QDVAAAHVVY ENASESDSGS RFGLIDTDVQ
//