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Database: UniProt
Entry: A0A0Q5R476_9SPHN
LinkDB: A0A0Q5R476_9SPHN
Original site: A0A0Q5R476_9SPHN 
ID   A0A0Q5R476_9SPHN        Unreviewed;       316 AA.
AC   A0A0Q5R476;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Molybdopterin dehydrogenase {ECO:0000313|EMBL:KQS04992.1};
GN   ORFNames=ASG11_12650 {ECO:0000313|EMBL:KQS04992.1};
OS   Sphingomonas sp. Leaf357.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS04992.1, ECO:0000313|Proteomes:UP000051080};
RN   [1] {ECO:0000313|EMBL:KQS04992.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04992.1,
RC   ECO:0000313|Proteomes:UP000051080};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS04992.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04992.1,
RC   ECO:0000313|Proteomes:UP000051080};
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:KQS04992.1}.
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DR   EMBL; LMPM01000001; KQS04992.1; -; Genomic_DNA.
DR   RefSeq; WP_055779746.1; NZ_LMPM01000001.1.
DR   AlphaFoldDB; A0A0Q5R476; -.
DR   STRING; 1736350.ASG11_12650; -.
DR   OrthoDB; 9814706at2; -.
DR   Proteomes; UP000051080; 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:SF5; ALDEHYDE OXIDOREDUCTASE FAD-BINDING SUBUNIT PAOB-RELATED; 1.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051080}.
FT   DOMAIN          1..223
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   316 AA;  33280 MW;  CAF188831C2A2BF2 CRC64;
     MKPFTYTRAT SPAEAAAAVA RTPGAKFIAG GTNLLDLMKL QIETPAHLID VQDLKLDRIE
     KTKDGGLRIG ALVKNTALAS DETVRRDYGV LSRSLLAGAS GQLRNKATTA GNLLQRTRCP
     YFYDTNQACN KRKPGSGCAA IGGFSRQLGV IGTSDACIAT HPSDMAVAMR VLDASVETVK
     ADGATRSIPM ADFHRLPGNT PHIETALMPG ELITAVTLPK PIGGMHLYHK VRDRSSYAFA
     LISVAAVVQQ DGTGRVAVGG VAHRPWRVEA AEADLPRGAR AVASGLLAGA KPSHENAFKL
     PLVERTLAAV LAEAKG
//
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