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Database: UniProt
Entry: M0AM67_NATA1
LinkDB: M0AM67_NATA1
Original site: M0AM67_NATA1 
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
//
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