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Database: UniProt
Entry: A0A0Q5TJ21_9SPHI
LinkDB: A0A0Q5TJ21_9SPHI
Original site: A0A0Q5TJ21_9SPHI 
ID   A0A0Q5TJ21_9SPHI        Unreviewed;       339 AA.
AC   A0A0Q5TJ21;
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:KQS35676.1};
GN   ORFNames=ASG14_09370 {ECO:0000313|EMBL:KQS35676.1};
OS   Pedobacter sp. Leaf194.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS35676.1, ECO:0000313|Proteomes:UP000051708};
RN   [1] {ECO:0000313|EMBL:KQS35676.1, ECO:0000313|Proteomes:UP000051708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf194 {ECO:0000313|EMBL:KQS35676.1,
RC   ECO:0000313|Proteomes:UP000051708};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS35676.1, ECO:0000313|Proteomes:UP000051708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf194 {ECO:0000313|EMBL:KQS35676.1,
RC   ECO:0000313|Proteomes:UP000051708};
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:KQS35676.1}.
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DR   EMBL; LMPU01000009; KQS35676.1; -; Genomic_DNA.
DR   RefSeq; WP_056871039.1; NZ_LMPU01000009.1.
DR   AlphaFoldDB; A0A0Q5TJ21; -.
DR   STRING; 1736297.ASG14_09370; -.
DR   OrthoDB; 9814706at2; -.
DR   Proteomes; UP000051708; 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:SF10; OXIDOREDUCTASE; 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;
FT   DOMAIN          1..223
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   339 AA;  36768 MW;  205E6611B1B49056 CRC64;
     MNNFEYKKAQ NVAESINLVA GRENTKFLAG GTNLVDLWKY NITNPDELVD VNHLDELLQI
     QTLPNGALRL GASVKNADTA YHPEVENRYP LLSKAILAGA SPQIRNMASN GGNLLQRTRC
     YYFYDAEVPC NKRIPGSGCP AKDGHNRIHA ILGTSEHCIA VFPSDMCVAL AALDAVVNVA
     GPAGTRAIAF ADFHRLPGDR PDLDNTLKPD ELITSIDLPD NNFATHYSYL KLRDRHSYAF
     ALVSVATALQ LDGDTIVDAR IALGGVAHKP WRSVAAENFL KGKEATTENF GKAADLILEG
     AKGFGNNDFK IKLAKKAIQR NCIMALNPDS QEPGAQPSA
//
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