ID   A0A0F2PPR7_9FIRM        Unreviewed;      1014 AA.
AC   A0A0F2PPR7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Heterodisulfide reductase {ECO:0000313|EMBL:KJS15450.1};
GN   ORFNames=VR69_13440 {ECO:0000313|EMBL:KJS15450.1};
OS   Peptococcaceae bacterium BRH_c4b.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS15450.1, ECO:0000313|Proteomes:UP000033446};
RN   [1] {ECO:0000313|EMBL:KJS15450.1, ECO:0000313|Proteomes:UP000033446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS15450.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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 HdrA family.
CC       {ECO:0000256|ARBA:ARBA00006561}.
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:KJS15450.1}.
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DR   EMBL; LADO01000052; KJS15450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2PPR7; -.
DR   STRING; 1629717.VR69_13440; -.
DR   PATRIC; fig|1629717.3.peg.186; -.
DR   Proteomes; UP000033446; Unassembled WGS sequence.
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   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR039650; HdrA-like.
DR   PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR   PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR   Pfam; PF00037; Fer4; 2.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 3.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          106..135
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          941..970
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          971..999
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1014 AA;  111725 MW;  BEEF5C40C89A9994 CRC64;
     MNSNKNTETN KTGAVLVVGA GISGMQSALD LAEMGYKVYI VEKTPAIGGK MPMLDKTFPT
     NDCSMCILSP KLVECGRHRN IEVLTMSEVM DLQGEPGRYK VTVKKYPRFV DTGKCTGCGS
     CAEECPVKMD DPFNQNLGKR KAIYKLYPQA YPNAYVIDQS KCLKLKNPKA CGKCLEACQA
     GAIDHKMQGE EVTLEVGAVI LCSGFELFDA EIRGEYGYGV YDNVITSLQF ERMLSASGPF
     RGHVQRPSDG KEPKKIAFIQ CVGSRDICND QGYCSSVCCM YATKEAIIAR EHVPGLDTTI
     FCIDVRAYGK DFEKYYNRAK NDYDVRYIKS MISSVKELQQ SNDLRLRYRT PDGSIVDEDF
     DMVVLSVGLK PTKDALELSE IMRIELNHYN FCQLKELTGV ETSREGIYVA GAFSGPKDIP
     ETVMQASAAA GDCATYLADA RNTLVTEKKF PEEIDIADQD TRIGVFVCHC GINIGSVVDV
     PSVVEYAKTL PNVVHAQEGL YVCSQDSQAA MRQLIDELKL NRIVVASCSP RTHKPLFQET
     MREAGLNKQL FEMANIRDQC SWVHQTEPEK ATLKSKDLVK MAVAKAATQK PIKPIIVQVT
     PAALVIGAGI AGINTALCLA DQGFQVHLVE KTDRLGGIAN RIREGYNGED IPAYLNKLID
     RINSNPRISL FTNCQVSGVS GYVGNFNTKL TNGQTISHGA TIITTGGEET KPTEYLYGKD
     SRVLTQLELD EAIKNNSQTL REAKNIVMIQ CVGSREAHRP YCSRICCTKT MRLALKLKEI
     NPDTNIVVLY RDIRTYGFNE DYYREARAKG VFFIRYEVDN KPLVEQVDKD GKQVIQVSVT
     DHILGDTIKI DADLMVLAAA SVPPETNQAL SQIFKVPLNP DAFFLEAHMK LRPVDFASDG
     IFMAGLAHGP KSVEESIAQS KAAAGRAATV LGRKTLESKG ITARVDPDKC AACLTCVRLC
     PYNAPRIKEH KAEIEAVICQ GCGSCAGECP NKAIVLEGYS DKQYLTMVNS LFEQ
//