ID A0A090AGX3_9GAMM Unreviewed; 475 AA.
AC A0A090AGX3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:BAP54492.1};
GN ORFNames=THII_0195 {ECO:0000313|EMBL:BAP54492.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP54492.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP54492.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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DR EMBL; AP014633; BAP54492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AGX3; -.
DR STRING; 40754.THII_0195; -.
DR KEGG; tig:THII_0195; -.
DR HOGENOM; CLU_001681_9_0_6; -.
DR OrthoDB; 9775084at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0071949; F:FAD 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; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
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; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR45444:SF3; ALDEHYDE OXIDASE_XANTHINE DEHYDROGENASE, MOLYBDOPTERIN BINDING PROTEIN; 1.
DR PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623}.
FT DOMAIN 1..84
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 168..357
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 475 AA; 52354 MW; A0D400575ECDE983 CRC64;
MVNFILNDKD ISTDVFEGTC ILDFLRHNQR LVGTKTGCQE GDCGACLILV GEWKGHLISY
QSANSCLLSL GQVNGKHVIT IEGLNQTDLT PIQQALLTEG ATQCGYCTPG IVLAITGLFF
NSSHFDSAQQ LAAVDGNLCR CTGYQAIKRA LIRVCQQLLS TASSLNHSKI ERIAWLVEKQ
IVPAYFLQIP QRLQKYQLPA KPITTEMASV GTFIAGGTDL WTQPIDTSQP LIYLSPDKSL
KGIHIEKNRC YIGAATTVEE IKNSPIIQAF FPKMTAYFKL IAATPIRHQA TIGGNIVHAS
PIGDLTILFL VLETTLHLNS GHTQRTLALK DFFTGYRQVN KQPHEWVESL SFSLPSKHVL
VNFEKVSKRT HLDVASINSA IQIHVEKDLI QQLHLSAGGV APIPLYLAQT VNYLSGKKVT
AATIRQAVTV AQTEITPLSD VRGSAEYKRL LLRQLIYAHF ITLFPEQITL EALLP
//
