ID U1Q8C2_9EURY Unreviewed; 341 AA.
AC U1Q8C2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=J07HN6_00853 {ECO:0000313|EMBL:ERH02808.1};
OS Halonotius sp. J07HN6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halonotius.
OX NCBI_TaxID=1238427 {ECO:0000313|EMBL:ERH02808.1, ECO:0000313|Proteomes:UP000030638};
RN [1] {ECO:0000313|EMBL:ERH02808.1, ECO:0000313|Proteomes:UP000030638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HN6 {ECO:0000313|Proteomes:UP000030638};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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}.
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DR EMBL; KE356567; ERH02808.1; -; Genomic_DNA.
DR AlphaFoldDB; U1Q8C2; -.
DR HOGENOM; CLU_042088_3_1_2; -.
DR Proteomes; UP000030638; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030638}.
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 152..153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 233..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ SEQUENCE 341 AA; 35890 MW; 458A0D7A8D7DCDF5 CRC64;
MHTLLLDSDD VGANAPLAAV VPAIEAAFGA YERGDAQMPA KSYIDLPQYN GDFRSMPAYL
HVDGDAVETA DAADDWDAAG VKWVNVHTDN SERGLPTVMG TMIYSDPETA FPLAIMDGRE
LTRLRTGAAA AVATDHLAVE DATSLGIVGA GVQSYTQLEA IATVRPIEEV VIADRNPERV
ADFIDQFADR FDIRGGEISE AAACDVLSTV TPVESPLVDR DAVGDHTHIN AIGADAEGKH
ELSDEILLDA TLVIDDYEQT THSGEINVPY SAGALTDSDL DASLGEIVVG NKAGRTSDDG
LTVFDSTGLA IQDVAAAHVV YTEADENDNG SAFDLLGLAD S
//
