ID A0A1H7Y4Z8_9BACT Unreviewed; 554 AA.
AC A0A1H7Y4Z8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Thioredoxin reductase (NADPH) {ECO:0000313|EMBL:SEM40259.1};
GN ORFNames=SAMN04488505_104290 {ECO:0000313|EMBL:SEM40259.1};
OS Chitinophaga rupis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=573321 {ECO:0000313|EMBL:SEM40259.1, ECO:0000313|Proteomes:UP000198984};
RN [1] {ECO:0000313|EMBL:SEM40259.1, ECO:0000313|Proteomes:UP000198984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21039 {ECO:0000313|EMBL:SEM40259.1,
RC ECO:0000313|Proteomes:UP000198984};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOBB01000004; SEM40259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7Y4Z8; -.
DR STRING; 573321.SAMN04488505_104290; -.
DR OrthoDB; 109585at2; -.
DR Proteomes; UP000198984; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000198984}.
FT DOMAIN 5..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 554 AA; 61263 MW; 96092AB73FBC4AC3 CRC64;
MEQPLIFCID DDEQVLRAIV RDLKSQYRKN YKIISTTTVN EALDSLLELK NKGETIAMFI
SDQRMPVMEG VDFLEKAMQF YPEARRVLLT AYSDTDAAIK AINSVQLDYY LVKPWGPPEE
KLYPVIDELL DDWQHIYHPV FKGIKVVGYQ FSQQSHAVKD FLAGNLIPYQ WLDVQTTSDA
NRLLELNNLS LKELPVVFFE DGSYLVTPTI MEIAGKVGLN PHVKHDVYDV VIIGAGPAGL
AAGVYGASEG LKTLLIERRA PGGQAGTSSR IENYLGFPTG LSGAELTRRA IAQATRLGTE
FITPQSVKDI QQKDGYNKII LEDDSVINTR SVIITTGVDY RKLDTQGVDQ FTGAGIYYGA
AMTEATACKD KEVYIVGGGN SAGQAAMYLS KFAKNVYILI RKDDLSSTMS AYLIEQIKGA
SNIKIRPRTE IAEAIGTDKL EKLVIKNVET GETCTEAADA LYIFIGAKPF TDWIALNIIK
DDKGFIETGR ELKKYDAFGK IWKQQRDPYL LETSCPGIFA AGDVRASAMN RVAAAVGEGS
MAISFVHKYL AEVK
//
