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Database: UniProt
Entry: A0A1K1MBL8_9FLAO
LinkDB: A0A1K1MBL8_9FLAO
Original site: A0A1K1MBL8_9FLAO 
ID   A0A1K1MBL8_9FLAO        Unreviewed;       399 AA.
AC   A0A1K1MBL8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE            EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN   ORFNames=SAMN02927921_00543 {ECO:0000313|EMBL:SFW20501.1};
OS   Sinomicrobium oceani.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sinomicrobium.
OX   NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW20501.1, ECO:0000313|Proteomes:UP000182248};
RN   [1] {ECO:0000313|EMBL:SFW20501.1, ECO:0000313|Proteomes:UP000182248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW20501.1,
RC   ECO:0000313|Proteomes:UP000182248};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FPJE01000002; SFW20501.1; -; Genomic_DNA.
DR   RefSeq; WP_072315826.1; NZ_JAPPSR010000028.1.
DR   AlphaFoldDB; A0A1K1MBL8; -.
DR   STRING; 1150368.SAMN02927921_00543; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000182248; 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:UP000182248}.
FT   DOMAIN          32..165
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          177..324
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   399 AA;  43947 MW;  4C3FCD3BB177B945 CRC64;
     MIVASSPFTR QQLLPQEEML EVLKQKGELF IGIPKEIAYQ EKRVCLTPDA VNALTAHGHR
     VIIESNAGEG ANFTDREYSE AGAEVTNDVK KIYSCPIILK VEPPSRDELK LINPQTILIS
     ALQIKTQNKK YFEELAKKRI TAIAFEYIRD EDGNYPAVRS LSEIAGTASV LIAAELMTNA
     NNGNGLMFGN ISGVPPVDVV ILGAGTVGEF AARSALGLGA NVKIFDNSIT RLRRIQTHLG
     RPMHTSTLQP KNLFKALRRC DVVIGAVRGT NRAPVIVTET MVENMKNGAV IIDVSIDMGG
     CFETSEVTTH DKPTFEKHGV VHYCVPNIPA RYSRTASVSI SNIFTPYLLK IGDEGGLENS
     LRFDRGLRNG LYFYHGILTN KTVAEWFNLS HSDINLLIF
//
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