ID V9HHK9_9CLOT Unreviewed; 556 AA.
AC V9HHK9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Putative alkyl hydroperoxide reductase F subunit {ECO:0000313|EMBL:EEH99001.1};
GN ORFNames=CSBG_02627 {ECO:0000313|EMBL:EEH99001.1};
OS Clostridium sp. 7_2_43FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=457396 {ECO:0000313|EMBL:EEH99001.1, ECO:0000313|Proteomes:UP000017809};
RN [1] {ECO:0000313|EMBL:EEH99001.1, ECO:0000313|Proteomes:UP000017809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_2_43FAA {ECO:0000313|EMBL:EEH99001.1,
RC ECO:0000313|Proteomes:UP000017809};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA Ambrose C., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Clostridium sp. 7_2_43FAA.";
RL Submitted (JAN-2012) 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:EEH99001.1}.
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DR EMBL; ACDK02000009; EEH99001.1; -; Genomic_DNA.
DR RefSeq; WP_008676991.1; NZ_JH815222.1.
DR AlphaFoldDB; V9HHK9; -.
DR STRING; 457396.CSBG_02627; -.
DR GeneID; 65398007; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG3634; Bacteria.
DR HOGENOM; CLU_031864_5_4_9; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000017809; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017561; AhpF_homologue_put.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR03143; AhpF_homolog; 1.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017809}.
FT DOMAIN 5..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 480..555
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
SQ SEQUENCE 556 AA; 60923 MW; DDB655EFE1B0849D CRC64;
MNKIYDLIII GGGPAGLSAG LYAGRARLNT LIIEKEHTGG QINSTAEIVN YPGIVKTTGP
NLTSDMRTQA ENFGVKFQTA DVIDVDLSGD VKIIKTNNGE IQGRAIIIAT GASPRKLGFP
GEIEYGGRGV AYCATCDGEF FKDLEVLVIG AGYAAAEEAI YLTRFAKKVI IVAREPEFTC
AKSIGDKVKA NKNIEIRFNT EVVEAIGDDV LRSVKLINNV TNERSEYFPP KEDGTFGIFV
FVGYEPQTKV FKDKIEMDRY GYILTNENME TNIKGVYAAG DLRPKLLRQV VTAVADGAIA
ATDAERYVAS EKERLGIIEE EVIEEKVENK NEVPTSNNKA LSGRSNLLND TLRNQLKGIL
SKIENNISLV SIVDESNKKS IELRDLVLDI SDLSDKISAV IYKKGENLEM ESKIHADKYP
VVALLNKDSN YSGVKFHGVP GGHELNSFIL AIYNLAGPGQ ALNEDLLNEI KSLSLDKKTN
IKVAVSLSCH VCPEVVTAAQ RIAIENPNIE TEMLDLSNFK DIKDKHKIMS VPALIINDSK
VYFGGKKLED IVQLLK
//