ID A0A0S8KGQ8_9CHLR Unreviewed; 927 AA.
AC A0A0S8KGQ8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=2Fe-2S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51085};
GN ORFNames=AMJ93_12045 {ECO:0000313|EMBL:KPL20395.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL20395.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL20395.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL20395.1};
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 -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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:KPL20395.1}.
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DR EMBL; LJUZ01000199; KPL20395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KGQ8; -.
DR PATRIC; fig|1703388.3.peg.2124; -.
DR Proteomes; UP000052016; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 927 AA; 99421 MW; 10BCE8B94076AD13 CRC64;
MTEVIEFTVN GRVIRAEGFD PNMTLLSYLR DVLYLTGAKN GCGQGHCGAC TVIVNGKAQR
SCLLRLGKAA GARIETVEAL AKGGQLHPLQ EAFIEAGAIQ CGFCTPGMLM AAKALLDRNP
DPTEHEIRQA LKDNLCRCTG YASILRAVKN AAHRMRTGDV TRPSAAAPTA AWQVVGESVT
RKDAWDKVTG TLKYADDLYT PGMLYARALR SAYPHAEVLG VDTSQAEKVP GVAAVLTADD
VPGLNRFGLI NADQPVLAND KVRYVGDAIA CVYAETVGAA EEALERIRVQ YRELEVVSTP
QRAMEPDAPL IHEQGNVLVE HHVRKGDVAA AFEQADVIVE NDYYTPFVEH AYLEPEACLA
IPDGEGGVTV QVGSQGPYVD HKQIVASLGL PEERVRVVHT PMGGGFGGKE DITVQILAAL
GVLHTGRPVK MVLPRPESMR VSTKRHAMWM HYKHAAALDG RLLAVEAQII GDTGAYGSVG
PAVLFRSATF GAGPYEVPNV KIDCYAVYTN NPPCGAMRGF GSPEAAFASD CQVDELAARL
GMDPFEFRLR NALQAGSITA TGHHVLESVG IKECLTAVRE SLSQDKLPEP SAGTRLGVGI
SAAYKNVGLG PGLDDRAGSI AELDRAGHLI VRGGCIDMGQ GQDTVMAQIA AQTLQVPYRD
VRIITGDTAT CPDSYMTTAS RATLLQGRSV HMAVTKLRDL LLQYAVSEYD LNRQTVDLKD
GQIVDPSTGT TLSLSELAQR AAEQGYALSA EAYYTAPECY DNLQFDEKLF QKDPEKYRVH
VAYCFCAQAC ILEVNESNGE VRVLKVIAAQ DVGKAIHPQN IHGQMEGGVV MGMGYGLTEE
FVVDHGYVVT DTLRKFKIPR ITDAPDIVTL IVENPHSLGP FGAKGMAELS LSSSAPAIAN
AIHDALGVRI RQLPITPAKI SAALRGS
//
