ID A0A0S8GKH9_9BACT Unreviewed; 990 AA.
AC A0A0S8GKH9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Heterodisulfide reductase {ECO:0000313|EMBL:KPK73528.1};
GN ORFNames=AMJ79_15075 {ECO:0000313|EMBL:KPK73528.1};
OS Phycisphaerae bacterium SM23_30.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK73528.1, ECO:0000313|Proteomes:UP000051901};
RN [1] {ECO:0000313|EMBL:KPK73528.1, ECO:0000313|Proteomes:UP000051901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_30 {ECO:0000313|EMBL:KPK73528.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK73528.1}.
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DR EMBL; LJUC01000255; KPK73528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8GKH9; -.
DR STRING; 1703411.AMJ79_15075; -.
DR PATRIC; fig|1703411.3.peg.2665; -.
DR Proteomes; UP000051901; 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; -; 4.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; 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; PF13237; Fer4_10; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
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 82..111
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 129..158
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 908..937
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 938..967
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 990 AA; 110517 MW; 2A4498F60DD7A0C3 CRC64;
MQAALDCANS GLKAYLLEEH PSIGGNMAQL DKTFPTNDCS ICMLSPKLVE VGRHFNIEII
AYADLEKVEG EPGNFKVTIN KRTRLVDEEK CNGCGDCEEA CPFKTLDVFN GELVERKAIY
RLYPQAIPNV YTIDQETCTK CKKCVKVCKA EAIDHEMTDK KVPLEVGAII YAGGYDFFDA
AQKPEYGFGR YPNVITSMQF ERILSASGPY AGHLERPSDR KAVKKIAWIQ CFGSRDVTCG
NDYCSSVCCM YATKEAIIAK EHAGDVEPAI FFIDMRAFGK GFEGFYNRAQ NDYGVRYIRS
QVSALKENPK NRNIFVRYIV GDNDSRIRIE EFDMVVLSVG LVAHRSTRKI AEICDLKCNR
FGFIESRPQQ PVLSRREGIF LSGTVSGPRD IPETVMQSSA AAALCGQLLA SVRGAEVTVK
QYPPELEVAE QKPRIGVFIC HCGSNIASVV DVEEVAQYIK KLEGVAHVEC NIYSCSQDSQ
VHIKEVIQQK NLNRVVVASC TPRTHEPLFQ ETMRQAGLNK YLFEMTDIRE QCSWVHQQEP
EKATDKAKDL IRGSVGKSRL LVPLEFKKVG VTKEALIVGG GISGMTAALS LANQDFQAHL
VEKEPQLGGE LRHVKINLEG HNWQEYLENT IDQVQKHDKI KVYLDSEIDE VNGFVGNFTT
RLKGPNPVEI KHGVIIVATG AKEFKPDRFL YGQNEKVITQ RQLEEKLQGD FSPETVVMIQ
CVGSRDDERP YCSRICCGEA VKNALAIKEK NPDTKVYILY RDIRTYEYKE LYYLQAREKG
VMFIHFPDDN YPQVSENAPG LKVSVRDTVI DETLDLQTDL VVLSAATVPE KENNQRLAEL
LKVPLSEDKF FMEAHVKLRP VDFANEGIYL CGLAHSPKYT EENITQALAA AGRAACTLNK
DSLEVGGVIS VIDEERCASC LTCLRECPYD APFINARGKA EIEAAKCQGC GNCVAACPAK
AIQLRTFTDD QLRALFRSIL KVEEAAEVCS
//