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Database: UniProt
Entry: A0A1I1BQT7_9BACT
LinkDB: A0A1I1BQT7_9BACT
Original site: A0A1I1BQT7_9BACT 
ID   A0A1I1BQT7_9BACT        Unreviewed;       403 AA.
AC   A0A1I1BQT7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE            EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN   ORFNames=SAMN04489723_11670 {ECO:0000313|EMBL:SFB52745.1};
OS   Algoriphagus aquimarinus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=237018 {ECO:0000313|EMBL:SFB52745.1, ECO:0000313|Proteomes:UP000198790};
RN   [1] {ECO:0000313|EMBL:SFB52745.1, ECO:0000313|Proteomes:UP000198790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23399 {ECO:0000313|EMBL:SFB52745.1,
RC   ECO:0000313|Proteomes:UP000198790};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOKK01000016; SFB52745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1BQT7; -.
DR   STRING; 237018.SAMN04489723_11670; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000198790; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198790}.
FT   DOMAIN          32..165
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          177..325
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   403 AA;  43967 MW;  AB70E4D0F3E40621 CRC64;
     MPAEIDQLTA VGLIPKESPA KVRKNDYTLV VGLPKERSTQ EKRIVITPES VGLLSNNGIS
     VVVEAGAGLQ SKFTDQDFSD AGAKVTSSKK EVFESDVVLK IDPPTQEELE YMNQGSCLMS
     ALQLEGQDQE FIQTLNRKKI TAVAFEYLED KVGGMPVVRA MSEIAGSTVM LIAAEYLSSE
     NNGKGLIMGG VTGVPPTQVV IIGAGTVAEY AARTALGLGA NIKVFDNHIY KLRRLKQLLG
     QQIYTSTIDN FSLNQALSEA DVVIGALRAE KGRNKIVVSE EMVANMMHGS IIIDVAIDEG
     GCIETGKMTS HDEPVYQVHD IIHYCVPNIA SRVARTASYS LSNIFTPIIL QMADLGGAEE
     MIFNYKWFLR GVYTYRGSLT NAYMGRKFGI SHKELQLLLA ARY
//
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