ID A0A076HPM7_9BACT Unreviewed; 516 AA.
AC A0A076HPM7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=N008_04100 {ECO:0000313|EMBL:AII51163.1};
OS Hymenobacter sp. APR13.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1356852 {ECO:0000313|EMBL:AII51163.1, ECO:0000313|Proteomes:UP000028590};
RN [1] {ECO:0000313|EMBL:AII51163.1, ECO:0000313|Proteomes:UP000028590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APR13 {ECO:0000313|EMBL:AII51163.1,
RC ECO:0000313|Proteomes:UP000028590};
RA Li P., Jiang J., Kwok A.H.Y., Lou X., Xu D., Leung F.C.C.;
RT "Complete genome sequence assembly of Hymenobacter sp. APR13.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP006587; AII51163.1; -; Genomic_DNA.
DR RefSeq; WP_044013923.1; NZ_CP006587.1.
DR AlphaFoldDB; A0A076HPM7; -.
DR STRING; 1356852.N008_04100; -.
DR KEGG; hym:N008_04100; -.
DR eggNOG; COG4630; Bacteria.
DR HOGENOM; CLU_001681_9_0_10; -.
DR OrthoDB; 9796880at2; -.
DR Proteomes; UP000028590; 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.
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; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; 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:UP000028590}.
FT DOMAIN 1..86
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 218..400
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 217..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 54784 MW; CB1E0D5F63D65968 CRC64;
MLEFILNDQP IRTHEAPASA LLDFVRYHEQ LKGTKIGCRE GDCGACTVLV GELSADGQTV
NYQSMTSCLT PLGNAAGKHI VTVEGINAAG SQLTPVQQAI VDEGGSQCGF CTVGFVMSLT
GHSLGSQPAT EKSTIAAIDG NICRCTGYKS LERAAAKLTA ELEQRPAENA LTWLSEKQFV
PAYFANIPAQ LAALRPAATQ AAEASAAASV AAAATPHANG GSAVSASPNG HTQSQNDHGH
DSPIRPFTHS LIGGGTDLLV QRLEELREQP GVRLLFDQPG RRGIRRETTG RVVLGAATTA
SHLLNSELLR GLLPKLPQYL KLVSSTPIRN MGTVAGNFIN GSPIGDLTIL FLALGASVTL
LDAAGHTREL ALPDLYLDYK KLAKAPDEQV IDISFPAPLA GDFFHFEKVS KRTHLDIASV
NSAAWLRVDN GIIQAARISA GGVGPVPLLL ARTSEFLQGR ELSAETLTAA NAVMQEEISP
ISDVRGTADY KRLLLRQLLW AHFLEFAPEL AVDELI
//