ID M0PMV6_9EURY Unreviewed; 352 AA.
AC M0PMV6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=C462_07557 {ECO:0000313|EMBL:EMA71401.1};
OS Halorubrum arcis JCM 13916.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1230455 {ECO:0000313|EMBL:EMA71401.1, ECO:0000313|Proteomes:UP000011528};
RN [1] {ECO:0000313|EMBL:EMA71401.1, ECO:0000313|Proteomes:UP000011528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13916 {ECO:0000313|EMBL:EMA71401.1,
RC ECO:0000313|Proteomes:UP000011528};
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:EMA71401.1}.
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DR EMBL; AOJJ01000054; EMA71401.1; -; Genomic_DNA.
DR RefSeq; WP_007994847.1; NZ_AOJJ01000054.1.
DR AlphaFoldDB; M0PMV6; -.
DR STRING; 1230455.C462_07557; -.
DR PATRIC; fig|1230455.3.peg.1455; -.
DR Proteomes; UP000011528; 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; 37296 MW; 03B217663C12B8E9 CRC64;
MQTLLLNADD VDENAEMDRV IDAVRGAFTA YERGDAKMPA KSYIDLPEYN GDFRSMPAYL
DVREEDVAEE TATGDGWDAA GIKWVNVHTD NPGDHDLPTV MGTMIYSDPE TAFPLAVLDG
TTLTMKRTGA AAAVATDHLA VPDASSLGIV GAGVQSYTQL EAIAAVRDIE EVVISDLDEE
RVADFVDAFE DRFDVRAGSI AEAGHCDVLS TVTPVETPIV GPEDVGEHTH INAMGADAEG
KHELADDLLL DATVVIDDHE QCTHSGEINV PYAAGTLTDD DIYGEIGEIV VGRRAGRPGT
PGTPADADGV SGVSVFDSTG LAIQDVAAAR VVYERADELD NGYPFDLLGL DG
//