ID W4M8E9_9BACT Unreviewed; 462 AA.
AC W4M8E9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ETSY2_18620 {ECO:0000313|EMBL:ETX06191.1};
OS Candidatus Entotheonella gemina.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC Entotheonella.
OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX06191.1, ECO:0000313|Proteomes:UP000019140};
RN [1] {ECO:0000313|EMBL:ETX06191.1, ECO:0000313|Proteomes:UP000019140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX PubMed=24476823; DOI=10.1038/nature12959;
RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT "An environmental bacterial taxon with a large and distinct metabolic
RT repertoire.";
RL Nature 506:58-62(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ETX06191.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZHX01000764; ETX06191.1; -; Genomic_DNA.
DR AlphaFoldDB; W4M8E9; -.
DR HOGENOM; CLU_017779_9_2_7; -.
DR Proteomes; UP000019140; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF118; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE (PRECURSOR); 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019140}.
FT DOMAIN 43..220
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 462 AA; 49350 MW; 331B7C4EDFA8A79D CRC64;
MSEDAIVQTL REAIDPAMIC TDDGTRAFMA RDALHPSRLP AGEPVQPVCV VQPRCTEDVA
VVLQIATAAK CPVVPVGGGS GLMGGASSVS PGIVLDLRQL QEIEIRPADR MAEVGAGVTI
KALNEAAEPH ELMCGHDPWT VAVATVGGTI STNSLGYLGG KYGAMGDQVL GLEAVLPTGE
VIRTRAVEKA STGPSLHPLL VGAEGCFGVI TRATLRLVPM PQTRILQAWA FRDFASGFAA
INAILDAGIR PGLLDYGDDE PSAAHDPPCT LMVSYEGPKA VAQAEAKAAA ALYAQYRGQL
SPRREAERFW QERHASGDAY ARTRAAGQPW NRQRPRFDYL HVALPPSAVL TYRRQCLELL
AQQKCQVHQS GLWDHAGLFS LSYSIGSGVS RQDIHHALLT ACQDLHGAME YCHGVGTRLA
GLMRREHGAG LDVLRRLKRD LDPNGILNPG KLALSSIDTE TA
//