ID A0A086A8R5_9FLAO Unreviewed; 397 AA.
AC A0A086A8R5;
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=IW15_09950 {ECO:0000313|EMBL:KFF13079.1};
OS Chryseobacterium soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF13079.1, ECO:0000313|Proteomes:UP000028705};
RN [1] {ECO:0000313|EMBL:KFF13079.1, ECO:0000313|Proteomes:UP000028705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF13079.1,
RC ECO:0000313|Proteomes:UP000028705};
RA Stropko S.J., Pipes S.E., Newman J.;
RT "Genome of Chryseobacterium soli DSM 19298.";
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:KFF13079.1}.
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DR EMBL; JPRH01000003; KFF13079.1; -; Genomic_DNA.
DR RefSeq; WP_034710839.1; NZ_JPRH01000003.1.
DR AlphaFoldDB; A0A086A8R5; -.
DR STRING; 445961.IW15_09950; -.
DR eggNOG; COG0686; Bacteria.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000028705; 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; 44179 MW; 433239EA9713AC7A CRC64;
MSTTNIFTPF TEEELMPQEE KLEVVKKGKQ FSIGIPKETC LHERRTCITP DAVQVLVEHG
HEIIIESGAG EGSFFADLSY SEAGAKITND PKEAFGQDLI LKINPPTEDE IDYMKPNTYL
VSALQINLRE KAYFLKLAEK KINAIAFEFI VDEYKQLSLV RLVGEIAGTV SILYASELLA
LSNGLMLGGI TGVRPAEVVV IGAGIVGEFA TKAAIGLGAS VRVFDNSLSK LRRLHTIVDS
RVPTSIIDPK EVSKALRRAD VVIGALPRLN MTPVVTEDMV MRMKKGSVII DITIDNGKVI
ETSELTTMEE PYIIKHGVIH CGLPNLTSRM PRSTTKAISN FFLSYILNYD EEGGFENMLI
RKNEMKQSLY MYKGRHTKKV ICDRFGLTYH DINLLIF
//
