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Database: UniProt
Entry: K1YNU4_9BACT
LinkDB: K1YNU4_9BACT
Original site: K1YNU4_9BACT 
ID   K1YNU4_9BACT            Unreviewed;       557 AA.
AC   K1YNU4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN   ORFNames=ACD_75C00585G0006 {ECO:0000313|EMBL:EKD38861.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD38861.1};
RN   [1] {ECO:0000313|EMBL:EKD38861.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD38861.1}.
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DR   EMBL; AMFJ01031254; EKD38861.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1YNU4; -.
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; -; 1.
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; 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; PF12838; Fer4_7; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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          485..514
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          516..545
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   557 AA;  60151 MW;  F46B7527C56EF530 CRC64;
     MKKKSGENTE QLRVGVFICD CGSNIAGHLD CKSVTEYAAT LPGVVFTKEN LYTCSESGIG
     EIQNAIKTNN LNRVVVASCS PRTHQPLFAS SCAEAGMNPY LFEMVNIRDQ CSWVHMGKRD
     IATAKAKDLV RMGVAKSTTL EPQDNIESSL VRKILVIGGG IAGLSAAESL AGMGLEVLLV
     EKEQQLGGLM LDLNVLENGA DAKDRVTTLA EKVRATSGIT VFTGAKVTEI TGYIGNFQVT
     VQKPDEKIEE KVGCIVVASG AVPLTQEGLF GYNGRDVITQ MELERRLKDG SFKASKVVMI
     QCAGARNSTR EYCSRICCAT AVKNSMIIKR KSPLAEVHVL YRDMQMYGDV KEQMLWDARG
     MGVKFDVYDA LKPPVVSAGK VTFHHAVLGE TKEFPCDLVV LSTPLVARPD SPEVAALMRI
     PSDKNGFFLE AHAKLRPLDF AADGIFVCGS ARYPVTSVEA RTQGMGVASR VGAILFKDKL
     VKSGIVAEID AETCVGCMGC LNVCPYDAIS YNREKDVCEV KEILCKGCGN CASTCPSHSA
     VLRGYKPEQL LAQIRAI
//
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