ID A0A495SMJ0_9FLAO Unreviewed; 407 AA.
AC A0A495SMJ0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=C8C88_2502 {ECO:0000313|EMBL:RKT00670.1};
OS Flavobacterium sp. 123.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2135627 {ECO:0000313|EMBL:RKT00670.1, ECO:0000313|Proteomes:UP000271452};
RN [1] {ECO:0000313|EMBL:RKT00670.1, ECO:0000313|Proteomes:UP000271452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123 {ECO:0000313|EMBL:RKT00670.1,
RC ECO:0000313|Proteomes:UP000271452};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
RL Submitted (OCT-2018) 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:RKT00670.1}.
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DR EMBL; RBXD01000001; RKT00670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495SMJ0; -.
DR Proteomes; UP000271452; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000271452}.
FT DOMAIN 40..173
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 185..332
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 407 AA; 44722 MW; A5D34E3EE4E07D1F CRC64;
MHSNLTLPMS IIITPFTKLQ LLPQEEKLEI ARRKSELFIG IPKETSYQER RICLTPDAVN
SLTCHGHRVM IESGAGESSS YSDKEYSDAG AEVTQDTKKV FSCPMILKVE PASVAEIEMM
NPKTILISAI QIKTRKKAYF EALSKKKITA LAFEYIKDED GTYPAVKSLS EIAGTASILI
AAELMITNEF GKGLLFGNIT GVPPTDVVIL GAGTVGEFAA KTAIGLGANV KVFDNSITKL
RRLQNNLNQR IFTSTIQPKS LLKALRRCDV AIGAMRGLER CPVVVTETMV EHMKRGAVIV
DVSIDTGGCF ETSEVTSHEK PTFIKNNVLH YCVPNIPSRY SKTASLSISN IITPYLMQIA
EYGGIESALR CDKGLKNGVY MYHGILTNKA IGEWFELPDS DINLIVF
//
