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Database: UniProt
Entry: A0A080N422_9BIFI
LinkDB: A0A080N422_9BIFI
Original site: A0A080N422_9BIFI 
ID   A0A080N422_9BIFI        Unreviewed;       350 AA.
AC   A0A080N422;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=NAD-dependent oxidoreductase {ECO:0000313|EMBL:KFF30985.1};
DE            EC=1.1.1.179 {ECO:0000313|EMBL:KFF30985.1};
DE            EC=1.3.1.20 {ECO:0000313|EMBL:KFF30985.1};
GN   ORFNames=BBOMB_0314 {ECO:0000313|EMBL:KFF30985.1};
OS   Bifidobacterium bombi DSM 19703.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF30985.1, ECO:0000313|Proteomes:UP000028730};
RN   [1] {ECO:0000313|EMBL:KFF30985.1, ECO:0000313|Proteomes:UP000028730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF30985.1,
RC   ECO:0000313|Proteomes:UP000028730};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA   Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA   Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT   "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL   Appl. Environ. Microbiol. 80:6290-6302(2014).
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC       {ECO:0000256|ARBA:ARBA00010928}.
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:KFF30985.1}.
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DR   EMBL; ATLK01000001; KFF30985.1; -; Genomic_DNA.
DR   RefSeq; WP_044086500.1; NZ_JDTS01000001.1.
DR   AlphaFoldDB; A0A080N422; -.
DR   STRING; 1341695.BBOMB_0314; -.
DR   eggNOG; COG0673; Bacteria.
DR   OrthoDB; 9815825at2; -.
DR   Proteomes; UP000028730; Unassembled WGS sequence.
DR   GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR22604; OXIDOREDUCTASES; 1.
DR   PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:KFF30985.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028730}.
FT   DOMAIN          18..141
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   350 AA;  38014 MW;  213E8F723CC5139A CRC64;
     MSKLNGKREQ ARSEGLKVNV AILGAGSIAN AMAETLNAMT HTREYGGLVN LYAVAARDAG
     RAAQFASRYG LPVSYGSYAE LLADPDVDLI YIATPHSLHA EQGLACIEAG KNILVEKAFT
     ANASQAQELL TAAERSGLLC TEAIWPRYMP SRAIIDDILE SGAIGEVKAA SANLGYPTHY
     KKRITDPNLA GGALLDVGVY TLNFVDMALS DRSQRHIDRI ETSMLPYETG VDAHDSITLY
     YDDGVMATNA ASMLAVSDRT GTVWGTDGYL IVQNVNNPES IDVFDKEHHM AKHYAVPRQL
     TGYEYEVAAA ANAVLDGETE CTQMPHADTL RIMELMDSIR GEWGLKYPFE
//
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