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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//