ID A0A1F8MGI6_9CHLR Unreviewed; 660 AA.
AC A0A1F8MGI6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Disulfide reductase {ECO:0000313|EMBL:OGN97710.1};
GN ORFNames=A2Z77_04945 {ECO:0000313|EMBL:OGN97710.1};
OS Chloroflexi bacterium RBG_13_51_36.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797625 {ECO:0000313|EMBL:OGN97710.1, ECO:0000313|Proteomes:UP000179678};
RN [1] {ECO:0000313|EMBL:OGN97710.1, ECO:0000313|Proteomes:UP000179678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN97710.1}.
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DR EMBL; MGMS01000010; OGN97710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MGI6; -.
DR STRING; 1797625.A2Z77_04945; -.
DR Proteomes; UP000179678; 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 Gene3D; 3.30.70.20; -; 2.
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; 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; PF12831; FAD_oxidored; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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 236..266
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 586..615
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 617..646
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 660 AA; 72327 MW; B39A1CD3E4394FAA CRC64;
MEEIRIGVYI CHCGVNIAAT VDVAEVARYA GTLPGVVLSR DYVFMCSDPG QDLIRKDIKE
YNLNRVIVSS CSPRLHELTF RRVCESAGLN RYLFEMVNIR EQCSWTNEDK EANTEKAKAL
VDAAVRRVHY QEPLEIKDAP YNPNTLIVGG GIAGIQAALE IANSEHKVYL VEREPSIGGH
MIQLDKTFPT LDCSQCILTP KMSEVGSHPY IELLTYSEVE EVSGYVGNFK AKIRKKARHV
DVSKCTGCAV CMQKCPYKTD SEFELGLAKR KAAYIPFPQA VPNVATVDPN ICIYIKSEGK
KCGACIKSCE AGAITAETLL HQTDEIIEVE VGSIILATGF TTMDPKLIPQ YGYGKYDNVI
TGLEFERIVS PTGPTGGKIQ LKDGKEPESV AIVHCVGSRD KNYHEYCSRI CCMYALKQAN
YIKEELPDAD VYQLYIDMRC FGDGYEEFYN RLSSAGVNFV RGKVAQVTDQ AINDEEAGKL
IVVAEDTLLG RMLRIPVDMV ILCNAVEPQA DAGEVAKRFT INRKATGFFL ERHPKLDPVA
TPTEGTFVAG CCQSPKDIPD TVAQASAAAA RVLSLISKGR ITLEAAVSVI DEEKCSGCRI
CNLLCPYGAI SFIEDEKKSR INEALCKGCG TCGAACPSGA ITARHFTNEQ ILAQVEALVS
//
