ID A0A086AWE3_9FLAO Unreviewed; 397 AA.
AC A0A086AWE3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=IW22_11930 {ECO:0000313|EMBL:KFF21007.1};
OS Chryseobacterium sp. JM1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1233950 {ECO:0000313|EMBL:KFF21007.1, ECO:0000313|Proteomes:UP000028731};
RN [1] {ECO:0000313|EMBL:KFF21007.1, ECO:0000313|Proteomes:UP000028731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM1 {ECO:0000313|EMBL:KFF21007.1,
RC ECO:0000313|Proteomes:UP000028731};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Chryseobacterium sp. JM1.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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:KFF21007.1}.
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DR EMBL; JPRN01000005; KFF21007.1; -; Genomic_DNA.
DR RefSeq; WP_034726603.1; NZ_JPRN01000005.1.
DR AlphaFoldDB; A0A086AWE3; -.
DR eggNOG; COG0686; Bacteria.
DR Proteomes; UP000028731; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR CDD; cd05305; L-AlaDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008141; Ala_DH.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE 1; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 34..167
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 179..322
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 397 AA; 44180 MW; 6749E0840A4968A5 CRC64;
MSTTNIFTPF TEEELMPKEE KLEVIKKGKQ FSIGIPKETC LNERRTCITP DAVQVLVEHG
HELIIEAGAG EGSFFTDLQY SESGAKITTD PKEAFGQDLI LKINPPTEDE IDYMKPNTYL
VSALQINLRD KAYFLKLAER KINAIAFEFI VDEYKQLALV RLVGEIAGTV SVLYASELLA
LSNGLMLGGI TGVRPAEVVI LGAGIVGEFA TKAAIGLGAS VRVFDNSLSK LRRLHTLVDS
RVPTSIIDPK ELSKALRRAD VVIGALPRLN MTPIVTEEMV AKMKKGSVII DITIDNGKVI
ETSELTTMED PYIIKHGVIH CGLPNLTSRM PRTTTKAISN FFLSYILNYD EEGGFENMLI
RKNEMKQSLY MYKGRHTKKV ICDRFGLTYH DINLLIF
//
