ID A0A136MVW3_9BACT Unreviewed; 336 AA.
AC A0A136MVW3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=1,5-anhydro-D-fructose reductase {ECO:0000313|EMBL:KXK37906.1};
DE EC=1.1.1.292 {ECO:0000313|EMBL:KXK37906.1};
GN Name=afr_2 {ECO:0000313|EMBL:KXK37906.1};
GN ORFNames=UZ16_OP3001001019 {ECO:0000313|EMBL:KXK37906.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK37906.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK37906.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK37906.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK37906.1}.
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DR EMBL; LMZT01000048; KXK37906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MVW3; -.
DR STRING; 1617433.UZ16_OP3001001019; -.
DR Proteomes; UP000070296; Unassembled WGS sequence.
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; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43377; BILIVERDIN REDUCTASE A; 1.
DR PANTHER; PTHR43377:SF1; BILIVERDIN REDUCTASE A; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KXK37906.1}.
FT DOMAIN 6..123
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 137..329
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 336 AA; 36608 MW; 53A0CCF4A2B92986 CRC64;
MSGSRLRIGV SGCGGIASCI FKECQGLECI EVVAGYDPNP SKMAAFQEVA PCEIAATYED
LLSRKDIDAI VLAAPPRERV SQALQAAATG KAVFIEKPLA LTVHDANGIV TACRKAGVPL
MVGQVLRYFG GFRRMAEKVR AGEYGKIRAL QVNRISGPFP DFYRDAWRLK KETSGGLLFE
VHVHELDLSR YLCGNPKRVL AASKRIGQDP ETDYKDLYMG TIEFENGALG QYHFSHISAQ
GETSIRVFLD KGVARAGFGG AWFQPWEGDE VEIPASGDEE AAYRHEIRLF AEAVLRNEPV
AIPGEEGLWS VAMAEAMEKS AEKGVPVEIV NPIQSA
//