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Database: UniProt
Entry: A0A076HPM7_9BACT
LinkDB: A0A076HPM7_9BACT
Original site: A0A076HPM7_9BACT 
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
//
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