ID F3AF17_9FIRM Unreviewed; 860 AA.
AC F3AF17;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF0992_01662 {ECO:0000313|EMBL:EGG83390.1};
OS Lachnospiraceae bacterium 6_1_63FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658083 {ECO:0000313|EMBL:EGG83390.1, ECO:0000313|Proteomes:UP000004368};
RN [1] {ECO:0000313|EMBL:EGG83390.1, ECO:0000313|Proteomes:UP000004368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_1_63FAA {ECO:0000313|EMBL:EGG83390.1,
RC ECO:0000313|Proteomes:UP000004368};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_63FAA.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:EGG83390.1}.
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; ACTV01000017; EGG83390.1; -; Genomic_DNA.
DR AlphaFoldDB; F3AF17; -.
DR HOGENOM; CLU_333644_0_0_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000004368; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF12837; Fer4_6; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 463..540
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 708..738
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 739..769
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 860 AA; 93495 MW; 1AB2C6BE75935B42 CRC64;
MKILIIGGVA AGTKTAAKLK REDRSAEVTV ITKDRDISYA GCGLPYYVGG LIENREELIV
NTPAKYAGLT GVEVKTGKEA IALCADKKEV IVKDVETGAE EAYGYDKLVL TVGASPAKLP
IEGTDLSGVF QMRTPDDAEN IRSYVEENQV KKAVVIGAGF IGLEVAENLK AKGVQVTVID
FASQILPNIV DAEVAVYAKK HLLKEGIRVI TGTKADAIMG NDHVTGVKTS AGLLRCELLI
MAAGIRPNTD FLQDSGLEMF KGTILVDKTM KTNLEDVYAA GDCVMVTNRI TGKPQWSPMG
SSANLEGRTL AQVLTGTKKE YPGVLGTGVV KLPNLNIGRT GLTEEQAKNA GYDVVTVVAP
TDDKAHYYPD AGFFITKLIA DRESHKLLGV QVLGNGAVDK MVDIAVMGIN MGAVLEDFEN
ADFAYAPPFS TAIHPFVQAV YILLNKINGN LVSMTPAEYA AGKAKDYKVV DVGLTPSIRG
AVYVNLSQVN GEIEGLDKEE KLLLVCAKGK RGYFLQNRLR SYGYKNTVVL EGAQFFNDVK
VQHAENAVSP EEETRVKALG FLRDKTTLDK FNGRVITRNG KITADEARTI AEAAEMFGSG
EVTMTSRLTM EIQGVPFDNI EPLREYLMQA GLETGGTGSK VRPVVSCKGT TCQYGLIDTF
GLSEEIHERF FHGYSDVKLP HKFKIAVGGC PNNCVKPDLN DLGIIGQRIP QVDMEKCRGC
KICRVEKNCP INVAKVVDGK IVIDENSCNH CGRCIGKCPF NAFEDYTNGY RIYIGGRWGK
KVAQGRYLEK VFTDKEEVLS VVEKAILLFR EQGITGERFA DTVARIGFEN VQEQLLGDEL
LSRKEENIKA QKHLKGGATC
//
