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Database: UniProt
Entry: A0A0S8GRJ5_9BACT
LinkDB: A0A0S8GRJ5_9BACT
Original site: A0A0S8GRJ5_9BACT 
ID   A0A0S8GRJ5_9BACT        Unreviewed;      1076 AA.
AC   A0A0S8GRJ5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Ferredoxin {ECO:0000313|EMBL:KPK75654.1};
GN   ORFNames=AMJ79_10440 {ECO:0000313|EMBL:KPK75654.1};
OS   Phycisphaerae bacterium SM23_30.
OC   Bacteria; Planctomycetota; Phycisphaerae.
OX   NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK75654.1, ECO:0000313|Proteomes:UP000051901};
RN   [1] {ECO:0000313|EMBL:KPK75654.1, ECO:0000313|Proteomes:UP000051901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_30 {ECO:0000313|EMBL:KPK75654.1};
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   -!- 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:KPK75654.1}.
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DR   EMBL; LJUC01000130; KPK75654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8GRJ5; -.
DR   STRING; 1703411.AMJ79_10440; -.
DR   PATRIC; fig|1703411.3.peg.747; -.
DR   Proteomes; UP000051901; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          452..483
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          485..515
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1076 AA;  120099 MW;  34ED5A4E75C4F759 CRC64;
     MRKINKHPVL EIEPQEKVQF EYDGKKIEGE KGFTIAAALH QAGYPVHTHS LQNRNRSLEC
     GIGKCGACEM LVDGQIRRIC ITKADGVKKV QEIPRDYRPP VQSFQKDRPI NVYRTEVAII
     GAGPAGLAVR EVLNKHNICN IVIDNNDNIG GQFLMQTHQF FFFEKEKHFG GMRGYEIART
     LAGKDHTGIF LNSTVWDILQ GKRLAVKNIQ TEEIYYVEAQ YLVVATGAVP YMPTFENDDV
     PGVYTAAVVQ KMMNIEFTLL GKNVLTVGAG NIGYLTSYQL MQAGAKVKAI IEALDHEGGF
     PVQAHRVRRL GVPIICAHIL LKAIPNENYD GIVGAVVAEC ENFQPLPGTE KIIDGIDAIN
     ICTGLVSDDQ LLIKGNDIFG RNCLGAGDAI RIGEGTSAVL RGQQVAYEIL HDMGIPYNYD
     VYLRISKEYI DSQQEPIRVI EAPFEPTPQR RKKPFVLIDC LYGFACNPCA FACPHGAITK
     SSTSTVPEID FDKCVGCMQC VYLCPGLAIF GYNLKKDTLF LPIEYEAAEK AEVFLVDNNG
     RKLGEGIIEK IQRNENKTHV ARVKALNLHG DDLMDVRGFI VKEQYPEALE FKAHDQAIAS
     ESYICHCDDV KMDEILEVIG DRKFISVDEI KHTTRLGMGA CRGKRCIKRL KQSIKTYDKT
     VVGEATPRAP MSNQLAFGEL YPRKVHDKII TRLDGKANKV VKVRTLVAGG GIAGSALFRY
     LSEAQQQPVM INYGRGASWR NIAAGRPNFS LPELSDIAEH NHEIFKSLQK LKNIDYRPID
     YVTFAHDDRM YEALEASMAW SEARMIEPKD FQKLISPYIN PHLSTYQAAL IAKNCWQASP
     GKVVDLLRTI GIHHGGEVLE DCKLVDVEKD GGIYKALVQD HNKEYIEYQA QHFVNALGPA
     GSQFARRLGI ETGLFSVRHQ AFITRRLPFM GIEGVPLPML IDRRNYKGFT AVYGQQLGET
     GQIIGCASPA LEPAETGKNL KENSKEFLET ASEIFVSWIP QLSSVGFQAV WAGYYVEPRM
     ILDPDLGLFV GLRGQGFMLS QYLAQMYVDK LVGHEVPKYF DRLKLKGDGL LEKAFK
//
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