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Database: UniProt
Entry: A0A0S8I5D6_9DELT
LinkDB: A0A0S8I5D6_9DELT
Original site: A0A0S8I5D6_9DELT 
ID   A0A0S8I5D6_9DELT        Unreviewed;      1457 AA.
AC   A0A0S8I5D6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN   ORFNames=AMJ94_05395 {ECO:0000313|EMBL:KPK92290.1};
OS   Deltaproteobacteria bacterium SM23_61.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK92290.1, ECO:0000313|Proteomes:UP000051218};
RN   [1] {ECO:0000313|EMBL:KPK92290.1, ECO:0000313|Proteomes:UP000051218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_61 {ECO:0000313|EMBL:KPK92290.1};
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:KPK92290.1}.
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DR   EMBL; LJUR01000035; KPK92290.1; -; Genomic_DNA.
DR   STRING; 1703399.AMJ94_05395; -.
DR   PATRIC; fig|1703399.3.peg.4050; -.
DR   Proteomes; UP000051218; 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; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 5.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039650; HdrA-like.
DR   InterPro; IPR009051; Helical_ferredxn.
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; PF13237; Fer4_10; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF07992; Pyr_redox_2; 2.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 4.
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          109..139
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          1373..1402
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          1403..1432
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1457 AA;  159657 MW;  7E6114633F640661 CRC64;
     MEKGKEPQQK NAEKIGAVMV VGGGVGGMQA ALDLANSGFK VYLVEESSAI GGRMAQLDKT
     FPTNDCSMCT ISPKLVETGR HLNIQLMMDS EVMKVDGQAG NFSVTVRHKP RYIDISKCTG
     CSECAQVCPI ITPGRFDEGM AQQRAAYKLY PQAVPNAYAI EKLGVSPCRD ACPAGQRAQG
     YIALIREGRY DDAMRVIKED NPFPGICGRI CNHRCEEACN RNLVDQPLSI ASLKRFVADR
     VYAQPYLPPD PLPYNYEEKV AIIGAGPCGL TAAKDLRKLG YPVTIFEALP LAGGMLRVGI
     PDYRLPPQVV DREVREIVDL GIDLRLNTPV TDLDGVMNEG FKSVLIAVGA HEGRKLPIPG
     ANLPEVLINT QFLRDVSLSN IGIGSGNGHP HPKSIVQKRH VLVLGGGNVA MDCARTAVRL
     GAARVDMACL ESREKMPASM EEIHEAEEEG ITIYPSRSFK RVLDREGHVA GVEAVKVTFM
     EFDAEGRLNL ETEEGSEHLL PCEVVIFAIG QRAGLAFIPE SAGVGTTRMS TIAVNPNTYA
     ATRPGVFAAG DATTGTAYVI EAVAAGHKAA ASMHRYLRGE EMEPAPKPEL PVVKFTKDQI
     QERLVTGELK VTPRVKMAQS PAGQRVSSFR EVSLGYTEEE AKAEASRCLA CGICSECLSC
     VYKCGLNAIN HDMVETQEEV RVGSIILAPG YEVYNARLSQ EYGLGRYPNV LNALQFERIL
     SASGPTLGHV QRPSDGKAPR KIAFLQCVGS RDQNHPYCSA VCCMYATKEA IIAKEHEKEV
     EPTIFFIDIR AYGKGFDAYY ERARKEYGVR YVRCAISRVV EDPRTKNLRI TYLDEGGEMQ
     EEEFDLVVLS VGMVPAASTK ELAKNVEIEL DANGFAKTDP LDPLATTRPG VYVCGVFQGP
     KDIPETVAQA SGAAAAASQI LSEVRGTLVA RKEYPPQKEV KEEEPRIGVF VCHCGNNIGG
     VVNVPAVKEY AASLGAVVFA DENLYTCSQD TQEKIKKAIE EHKLNRVIVA SCTPRTHEPL
     FQETIREAGL NPYLFDMANI RDQCSWVHMH EKEVATSKAR DLVRMAVANA RLIRPLEELT
     KGVIKRGLVI GGGLAGMTAA LGLAGQGFEA VLVEKEAELG GNLRHLKTTL DGKDVSRYLE
     ELTARVTQHP RIQVFTNAVI TDFSGYVGNY KTSLMVGPRM FSRDVEHGVT ILATGGEEYK
     PKEYLYGQDQ RVLTQLEMEA FLHGDRRKIE ELKEVVMIQC VGSRNEERPY CSRVCCAEAV
     KNALTLKSLN PKARVVILYR DMRMYGTLEE DYARARKAGI RFLRYEEDRK PEVTQEDGRL
     RLTFYNPVLR ERLFLCGIAH SPKNIEESLS QASAAVSRAC TVLAKDEIQI SGVVSVVDPD
     KCAACLTCVR VCPYNVPVIN KDGVAEIEAA MCHGCGICAS ECPGKAIKLQ HFTDEQVMAK
     CDVIIEVLSD VFRGEQV
//
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