ID D3D9N6_9ACTN Unreviewed; 570 AA.
AC D3D9N6;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Cyclic nucleotide-regulated FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:EFC80377.1};
GN ORFNames=FrEUN1fDRAFT_6508 {ECO:0000313|EMBL:EFC80377.1};
OS Parafrankia sp. EUN1f.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC80377.1, ECO:0000313|Proteomes:UP000004777};
RN [1] {ECO:0000313|EMBL:EFC80377.1, ECO:0000313|Proteomes:UP000004777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1f {ECO:0000313|EMBL:EFC80377.1,
RC ECO:0000313|Proteomes:UP000004777};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA Fernandez M., Tisa L.;
RT "The draft genome of Frankia sp. EUN1f.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000849};
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:EFC80377.1}.
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DR EMBL; ADGX01000158; EFC80377.1; -; Genomic_DNA.
DR RefSeq; WP_006544371.1; NZ_ADGX01000158.1.
DR AlphaFoldDB; D3D9N6; -.
DR Proteomes; UP000004777; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 52..148
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 60534 MW; B1DA9637B43872C1 CRC64;
MQPSQEDIGG AGPAAAGQIT ETPDTHGAYP HLGVDQLAAL EAVGRRCPTT VGDLLFREGD
RTTDFFVVLS GLVASVDGYG TARERQISLH GERRFLGELS LLSGQTAFTS VVVRKSGEVL
AVPLDRLRRL VATDPGLGDL ILRAYLVRRW LLIGLGAGLR IVGSRYSPQA RRLRDFAARN
RLPHQWVCLE NDPSAEELLH TLAVEPADTP VVVWGRRVLR NPSIAELARA VGLPVPAHAG
STWDLIVVGA GPAGLAASVY GASEGLATVT LDCLATGGQA ATSPRIENYL GFPSGISGGD
LAERAVLQAE KFGACFSMPS RAVALGRNDG LHQVTLDNGE TLAARTVVIA TGAWYRELNV
PGLQEFEGTS VFRAATLVEA QTCRGDPVVV IGGGNSAGQA ALYLAQHAGF VRLCVRHGDL
SRDMSRYLVD QIVRIPSIEV RRHREISGLR GGSTLEAVIL EDKQTGAQEE VPARALFVFI
GARPHTDWLA DQVALDDRGF VRTGVDAEPA AEPSMAGDGS PDPCPLVLET SRRGVFAVGD
VRSGSVKRVA SAVGEGAMAV RLVHERLYRA
//
