ID A0A3S9P8F3_9BACT Unreviewed; 410 AA.
AC A0A3S9P8F3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=EI427_20115 {ECO:0000313|EMBL:AZQ64434.1};
OS Flammeovirga pectinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ64434.1, ECO:0000313|Proteomes:UP000267268};
RN [1] {ECO:0000313|EMBL:AZQ64434.1, ECO:0000313|Proteomes:UP000267268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12M1 {ECO:0000313|EMBL:AZQ64434.1,
RC ECO:0000313|Proteomes:UP000267268};
RA Bae J.-W., Jeong Y.-S., Kang W.;
RT "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT scallop, Patinopecten yessoensis.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; CP034562; AZQ64434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9P8F3; -.
DR KEGG; fll:EI427_20115; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000267268; Chromosome 1.
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:UP000267268}.
FT DOMAIN 38..171
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 183..332
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 410 AA; 44719 MW; 57525F10EEA1ACFD CRC64;
MGKQRDGFEK ATESYFQFHP QEVMEGPVNK KGNPIKIGIP KELNPDEKRC ALRPGAVSLL
VNNGCEVFVE TNTGRHINHS DTEYADAGAT IVYSHKEAME ADIVLKISAP TIEEISYMKQ
NKAIISAIHM RELKRDVLDT INKKKITALG FELIEDNVGG LPLVRAMSEI AGSTVMLIAA
EYLSSYNGGK GIILGGITGV PPSKVVILGA GTVAEYAART AIGMGAEVKV FDNAIYKLRR
LKKELGLPHL FTSAFDSTSL TEALSRADIA IGAVHTHGTR TPSIVTEEMV AVMRENSIII
DVCIDQGGCF ETSEPTNHRH PVYKKHGVIH YCVPNVASRV SRTATAAISN IFTTILNKLI
DEGSVDTMMR RHPWFTKGVY AYRGNITNQA LAEKFDLPLK NLDLILAAGI
//
