ID H5TX97_9ACTN Unreviewed; 575 AA.
AC H5TX97;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative two-component thioredoxin reductase {ECO:0000313|EMBL:GAB38105.1};
GN ORFNames=GOSPT_026_00110 {ECO:0000313|EMBL:GAB38105.1};
OS Gordonia sputi NBRC 100414.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB38105.1, ECO:0000313|Proteomes:UP000005845};
RN [1] {ECO:0000313|EMBL:GAB38105.1, ECO:0000313|Proteomes:UP000005845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB38105.1,
RC ECO:0000313|Proteomes:UP000005845};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL Submitted (FEB-2012) 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:GAB38105.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAFC01000026; GAB38105.1; -; Genomic_DNA.
DR RefSeq; WP_005203463.1; NZ_BAFC01000026.1.
DR AlphaFoldDB; H5TX97; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG0664; Bacteria.
DR Proteomes; UP000005845; 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 29..133
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 61509 MW; 2C07B1C4FFD5AA9D CRC64;
MSTRISSEDA PRLGDGQLVD DETPDTVGAF PRLTDAQVAT LETGGTRRSV HAGEVLIRAG
TRSSDFFVVL SGKVAIIDEG AEDGERRILR LHGPGRFLGE LGLLEGQVAF FTAEAIEDGE
VLVVPAERVR ELVAHDLVLS DLILRAYRIR RHLLIGLGAG FRIIGSCYSP DTLRLREFAM
RNRLPHKWID LEQDERAEQL LQSLGVAPED TPVVIWHGEK VLRNPTNAEL ARIVGLPVPD
SVPDAAQDVC DLVVVGAGPA GLAASVYGAS DGLNTVTLES IAAGGQASTS SRIENYLGFP
AGVSGAELAE RAIIQAGKFG ARLLVSADVA GLGSEAGHHV LRLADGGEIR ARAVVLATGA
RYRKLEVSGI EALEGRSVYY AATHQEARLC GTDPVAIVGG GNSAGQATVF LADHVSHVHL
LIRGGDLGKS MSRYLVDQIE RHPRVTVHRN TEIREVHGEK YLEEIVVEDN RTGDQDTIRV
HALFVFIGAM PHTGWLADTI ALDDHGFVLT GMDAVHARGD GNRPISAGLS RTLETSRAGL
FAAGDVRRGS VKRVASAVGE GAMAVRQIHE YFERS
//
