ID B1M2I9_METRJ Unreviewed; 316 AA.
AC B1M2I9;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Molybdopterin dehydrogenase FAD-binding {ECO:0000313|EMBL:ACB26229.1};
GN OrderedLocusNames=Mrad2831_4262 {ECO:0000313|EMBL:ACB26229.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB26229.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB26229.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001001; ACB26229.1; -; Genomic_DNA.
DR RefSeq; WP_012321183.1; NC_010505.1.
DR AlphaFoldDB; B1M2I9; -.
DR STRING; 426355.Mrad2831_4262; -.
DR KEGG; mrd:Mrad2831_4262; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_1_0_5; -.
DR OrthoDB; 9814706at2; -.
DR Proteomes; UP000006589; Chromosome.
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}.
FT DOMAIN 1..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 316 AA; 33180 MW; 182E250843275900 CRC64;
MKSFTYERPG TPAEAAAAVA ATPGAKFIAG GTNLLDLMKL QIETPRHLVD VNGLGLDAVE
PTEEGGLRIG ALVRNTDLAA HPRVRKDYGV LARALLAGAS GQLRNKATTA GNLLQRTRCP
YFYDTAQPCN KRQPGSGCSA LDGVSRQLAV IGASEACIAT HPGDMAVAMR VLDATVETID
AGGAARKIPI AEFHRLPGDE PQRDTNLGPG ELITAVTLPK PVAGTHIYRK VRDRASYAYA
LVSVAAILGK DGTGHVAFGG VAHKPWRVEA AEADLPKGAR AVTDRVFADA APTHENAYKL
KLAERTLGAA LNQARA
//
