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
//