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Database: UniProt
Entry: A0A0Q5TEP0_9BACT
LinkDB: A0A0Q5TEP0_9BACT
Original site: A0A0Q5TEP0_9BACT 
ID   A0A0Q5TEP0_9BACT        Unreviewed;       332 AA.
AC   A0A0Q5TEP0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=FAD-binding molybdopterin dehydrogenase {ECO:0000313|EMBL:KQS34066.1};
GN   ORFNames=ASG33_08595 {ECO:0000313|EMBL:KQS34066.1};
OS   Dyadobacter sp. Leaf189.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS34066.1, ECO:0000313|Proteomes:UP000051810};
RN   [1] {ECO:0000313|EMBL:KQS34066.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS34066.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS34066.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS34066.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQS34066.1}.
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DR   EMBL; LMPS01000001; KQS34066.1; -; Genomic_DNA.
DR   RefSeq; WP_056282591.1; NZ_LMPS01000001.1.
DR   AlphaFoldDB; A0A0Q5TEP0; -.
DR   STRING; 1736295.ASG33_08595; -.
DR   OrthoDB; 9814706at2; -.
DR   Proteomes; UP000051810; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR42659:SF1; BLR6160 PROTEIN; 1.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051810}.
FT   DOMAIN          1..226
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   332 AA;  35834 MW;  6D739B1EE9272418 CRC64;
     MKAFQYLRPS KVQDAIRAVG SDPGARFIAG GTNLIDLMKR GIVSPDKLVD INHLPLKKIS
     YQSGRLKIGA LALNSEVAAH PAVLQKQPLL AQALHSGASG QLRNMATMGG NALQRTRCPY
     FYDTAFPCNK RKPGSGCAAV EGINRMHSIF GVEKANATQS CIAVHPSDMS VALAALDAEV
     IIQGQGGERR IAFTDLHRLP GNQPELDTTL ERNELITGFE IPDNDFGMHA HYLKVRDRAS
     FAFAIVSVAA ALDVKEGKIN AARLAMGGVA HKPWRLFEAE RHLLGKPVSE ALFRQAAALG
     MRDAVSFGQN DYKLRMAPNA VVQALLHAAA IE
//
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