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Database: UniProt
Entry: A0A0G3ED41_9BACT
LinkDB: A0A0G3ED41_9BACT
Original site: A0A0G3ED41_9BACT 
ID   A0A0G3ED41_9BACT        Unreviewed;       445 AA.
AC   A0A0G3ED41;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=1,5-anhydro-D-fructose reductase {ECO:0000313|EMBL:AKJ64386.1};
DE            EC=1.1.1.292 {ECO:0000313|EMBL:AKJ64386.1};
GN   Name=afr_1 {ECO:0000313|EMBL:AKJ64386.1};
GN   ORFNames=L21SP4_01136 {ECO:0000313|EMBL:AKJ64386.1};
OS   Kiritimatiella glycovorans.
OC   Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC   Kiritimatiellaceae; Kiritimatiella.
OX   NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ64386.1, ECO:0000313|Proteomes:UP000035268};
RN   [1] {ECO:0000313|Proteomes:UP000035268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of the first cultured
RT   representative of the subdivision 5 of the Verrucomicrobia phylum.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKJ64386.1, ECO:0000313|Proteomes:UP000035268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Fru-AB {ECO:0000313|EMBL:AKJ64386.1,
RC   ECO:0000313|Proteomes:UP000035268};
RX   PubMed=27300277; DOI=10.1038/ismej.2016.84;
RA   Spring S., Bunk B., Sproer C., Schumann P., Rohde M., Tindall B.J.,
RA   Klenk H.P.;
RT   "Characterization of the first cultured representative of Verrucomicrobia
RT   subdivision 5 indicates the proposal of a novel phylum.";
RL   ISME J. 10:2801-2816(2016).
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DR   EMBL; CP010904; AKJ64386.1; -; Genomic_DNA.
DR   RefSeq; WP_052881721.1; NZ_CP010904.1.
DR   AlphaFoldDB; A0A0G3ED41; -.
DR   STRING; 1307763.L21SP4_01136; -.
DR   KEGG; vbl:L21SP4_01136; -.
DR   OrthoDB; 9792935at2; -.
DR   Proteomes; UP000035268; Chromosome.
DR   GO; GO:0033712; F:1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR043906; Gfo/Idh/MocA_OxRdtase_bact_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR   PANTHER; PTHR43818:SF5; OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF19051; GFO_IDH_MocA_C2; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:AKJ64386.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035268}.
FT   DOMAIN          43..167
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          218..444
FT                   /note="Gfo/Idh/MocA-like oxidoreductase bacterial type C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19051"
SQ   SEQUENCE   445 AA;  50254 MW;  B932D2AC8555A40E CRC64;
     MKKRRTGTNG LARRAFLRSA AALSSPLILP RGVRGMPAPS NRITVGFIGL GRHGFGVNLK
     SMLAQPDMEP VALCDVDTDY LKRAMDHVKS TREITLDRKA VTTDWREVIA RSDIDAVMIS
     TPDHWHVPIA LAALRAGKDV ICEKPTLTIE EGQVLRRTVR EYGRVFQGSM EDRAMPMYHR
     MAELVRNGHI GKLRHIGITV PGAPWSETPP RGQPPQFEVK SVPVPATLDY DMWLGPAPEA
     PYQPERVHYM NPAGGWRFIR DYSGGMLSDW GVHMGDTAQW ASNTESTGPI DVSGRGYFFR
     DGLYNTAHQF QVRYRYAEGF DMTIESGGTG IRFEGTDGWL EVSAWARPIQ ASDPTVLRHI
     TGPNEVRLYT DYSREHRNFL DCVKSRRDPY FPVEALHRVS TIVHLGNIAL QLERPLTWDP
     QQERFPDDAR ACSMMSREMR APWTL
//
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