ID S2ZKQ9_9ACTN Unreviewed; 293 AA.
AC S2ZKQ9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=HMPREF1527_01326 {ECO:0000313|EMBL:EPD77393.1};
OS Atopobium sp. oral taxon 199 str. F0494.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=1203602 {ECO:0000313|EMBL:EPD77393.1, ECO:0000313|Proteomes:UP000014384};
RN [1] {ECO:0000313|EMBL:EPD77393.1, ECO:0000313|Proteomes:UP000014384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0494 {ECO:0000313|EMBL:EPD77393.1,
RC ECO:0000313|Proteomes:UP000014384};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Tanner A.C.,
RA Dewhirst F.D., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Atopobium sp. oral taxon 199 F0494.";
RL Submitted (MAY-2013) 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:EPD77393.1}.
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DR EMBL; ATCH01000002; EPD77393.1; -; Genomic_DNA.
DR RefSeq; WP_016477905.1; NZ_KE150487.1.
DR AlphaFoldDB; S2ZKQ9; -.
DR STRING; 1203602.HMPREF1527_01326; -.
DR PATRIC; fig|1203602.3.peg.1300; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_0_1_11; -.
DR OrthoDB; 9793944at2; -.
DR Proteomes; UP000014384; 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; -; 1.
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; 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:UP000014384}.
FT DOMAIN 1..177
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 293 AA; 31503 MW; B7AF31EE97E226E1 CRC64;
MYDIESLYSA TSVDDAIRAL SEDPESIVVA GGTDVLVKIR EGKFAGAHLV SIHELHDELD
GVSLGADGTV EIGPITWFHH VTTSKVIQET VPVLGEACDT PGGPQLRVSG TIGGNVCNAA
TSADSASTLY AYGALLDVKG PEGARTIPIE EWYAGPGRST KKRDEILVKI RIPKSHYEGF
TGYYFKYGKR RALEIATMGC CCLVKLSADK KTVDDIRLAF GVAGPTPMRA LSTEEALRGM
PVVEAVEKIG ELAAGDTNPR DSWRASKEFR LQLIKEMSKR SFAEAARRGG AEL
//
