ID C2BFT6_9FIRM Unreviewed; 514 AA.
AC C2BFT6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Alkyl hydroperoxide reductase, F subunit {ECO:0000313|EMBL:EEI86196.1};
DE EC=1.8.1.- {ECO:0000313|EMBL:EEI86196.1};
GN Name=ahpF {ECO:0000313|EMBL:EEI86196.1};
GN ORFNames=HMPREF0072_1206 {ECO:0000313|EMBL:EEI86196.1};
OS Anaerococcus lactolyticus ATCC 51172.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525254 {ECO:0000313|EMBL:EEI86196.1, ECO:0000313|Proteomes:UP000005984};
RN [1] {ECO:0000313|EMBL:EEI86196.1, ECO:0000313|Proteomes:UP000005984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51172 {ECO:0000313|EMBL:EEI86196.1,
RC ECO:0000313|Proteomes:UP000005984};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000238-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000238-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:EEI86196.1}.
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DR EMBL; ABYO01000211; EEI86196.1; -; Genomic_DNA.
DR AlphaFoldDB; C2BFT6; -.
DR STRING; 525254.HMPREF0072_1206; -.
DR eggNOG; COG3634; Bacteria.
DR HOGENOM; CLU_031864_4_2_9; -.
DR Proteomes; UP000005984; Unassembled WGS sequence.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR CDD; cd03026; AhpF_NTD_C; 1.
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; IPR044141; AhpF_NTD_C.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR03140; AhpF; 1.
DR PANTHER; PTHR48105:SF6; ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000238-2}; FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EEI86196.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005984}.
FT DOMAIN 125..192
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 211..499
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 212..227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 473..483
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 340..343
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 514 AA; 54946 MW; BB1B81990671F8D7 CRC64;
MVKSNMLDTN LKNQLAQYFG LLKTEVTIGL SAHDEKSKKV REFVEEVVAL SDKVKLVEKD
LPYTPSFEIK GAFDHGRIIF AGLPLGHEFA SFALAMLQAG GIAPKIDDSD KKRIESLGPA
DFETIVSLSC HNCPDVVQAL NIMAILNPKI NHTMIDGGTF QDLAESRDVL AVPAIFKDGE
FFEGGKQSLA SLLDKLGTKV DKGEFANKGL FDTLIIGGGP AAATAAIYAA RKGIKTGLVA
SEFGGQVNET LSIENIPGFK YTEGPDFMVQ MKEQVTSLDV DLMTGVLADG IKAVSDKVEI
SLDNGAKLFA KTAIIATGAR WRLIGIPGET EFRNKGVAYC THCDGPLFKG KNVAVIGGGN
SGIEAAIDLA GIVKHVTVLE FLPELKADEI LQKKLKSLDN VKVITNAQTT GLYGEGKVER
LEYTDRVSGE ENKLDIAGCF IQVGLIPNTD WMGDSGIEKN KMGEIITGND GATNIERIYA
AGDATNSKFK QIVIAAGSGA TAALGAYNYL MVNE
//
