GenomeNet

Database: UniProt
Entry: M0EU56_9EURY
LinkDB: M0EU56_9EURY
Original site: M0EU56_9EURY 
ID   M0EU56_9EURY            Unreviewed;       352 AA.
AC   M0EU56;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=C464_01948 {ECO:0000313|EMBL:ELZ50618.1};
OS   Halorubrum coriense DSM 10284.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=1227466 {ECO:0000313|EMBL:ELZ50618.1, ECO:0000313|Proteomes:UP000011509};
RN   [1] {ECO:0000313|EMBL:ELZ50618.1, ECO:0000313|Proteomes:UP000011509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10284 {ECO:0000313|EMBL:ELZ50618.1,
RC   ECO:0000313|Proteomes:UP000011509};
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:ELZ50618.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AOJL01000012; ELZ50618.1; -; Genomic_DNA.
DR   RefSeq; WP_006111807.1; NZ_AOJL01000012.1.
DR   AlphaFoldDB; M0EU56; -.
DR   STRING; 1227466.C464_01948; -.
DR   PATRIC; fig|1227466.3.peg.392; -.
DR   OrthoDB; 21421at2157; -.
DR   Proteomes; UP000011509; 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        83
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         235..237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ   SEQUENCE   352 AA;  37223 MW;  A350E1848F077309 CRC64;
     MQTLLLNADD VDENAEMDRV IDAVRGAFTA YERGNAKMPA KSYIDLPEYN GDFRSMPAYL
     DVNEDDVAEE TATGDGWDAA GIKWVNVHTD NPADHDLPTV MGTMIYSDPE TAFPLAVLDG
     TTLTMKRTGA AAAVATDHLA VPDANSLGIV GAGVQSYTQL EAIAAVRDIE EVVVSDLDEE
     RVADFLDAFG DRFDVRAGSV SEAGHCDVLS TVTPVESPIV GPEDVGDHTH INAMGADAEG
     KHELADDLLV DATVVIDDHE QCTHSGEINV PYAAGTLTDD DIYGEIGEIV VGHRSGRPGT
     PGTPADADGV SGVSVFDSTG LAIQDVAAAR VVYERADELD NGYPFDLLGL DD
//
DBGET integrated database retrieval system