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Database: UniProt
Entry: R8APW6_PLESH
LinkDB: R8APW6_PLESH
Original site: R8APW6_PLESH 
ID   R8APW6_PLESH            Unreviewed;      1021 AA.
AC   R8APW6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=FAD linked oxidase {ECO:0000313|EMBL:EON88372.1};
GN   ORFNames=PLESHI_10895 {ECO:0000313|EMBL:EON88372.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON88372.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON88372.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON88372.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL   Genome Announc. 1:e00404-13(2013).
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:EON88372.1}.
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DR   EMBL; AQQO01000345; EON88372.1; -; Genomic_DNA.
DR   RefSeq; WP_010863787.1; NZ_KB944511.1.
DR   AlphaFoldDB; R8APW6; -.
DR   STRING; 703.SAMEA2665130_01682; -.
DR   PATRIC; fig|1315976.3.peg.2040; -.
DR   HOGENOM; CLU_010756_1_0_6; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000014012; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014012}.
FT   DOMAIN          48..281
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1021 AA;  113179 MW;  AC5585A9E14E3A7E CRC64;
     MIPQLSGVPG VAPLTHSFLS ALSAAGFSGD TDVTYGGRLS MATDNSVYQQ LPQAVLFPRS
     VADILLLTRT AQQAEFKELT FAPRGGGTGT NGQSLTTGVV VDTSRYMNRI LELNLEEKWV
     RVEAGVVKDQ LNAYLKPHGY FFSPDLSTSN RATIGGMINT DASGQGSLLY GKTSDHVLGL
     RAVMLDGSLL DTAPMPVEVA EQLAQQKDPI GRVYQTVLQR CRDQRELILA RFPKLNRFLT
     GYDLRHVFSD DLRQFDLTRL LTGSEGSLAF IAEAKLNITP IPKQRRLINI KYDSFDSALR
     HAPFMVAAQA LSVETVDSKV LNLAREDIVW HSVRELITDV PGCDMQGLNI VEYAGDDAEL
     IDAQVSDLCQ RLDTLLPSRE GGVIGYQVCH DLVDIERIYT MRKKAVGLLG NTKGAAKPIA
     FAEDTCVPPE HLADYIAEFR ALLDSQGLHY GMFGHVDAGV LHVRPALDLC DPEQERLMKT
     ISDQVVTLTA KYGGLMWGEH GKGFRSEYSP LFFGEALWAE LQQIKTVFDP DNRLNSGKIC
     TPLKAGAELV QVAGEKRSWH DRKIPLNVRE SYRGALECNG NGLCFNFDTH SPMCPSVKIT
     RDRRHSPKGR AALVREWLTM LADEGADVLG LEQQLAGSSF SFRELMDKTR YTLAARRGEY
     DFSHEVKEAM AGCLACKACS TQCPIKIDVP AFRARFLQLY HTRYLRPARD YMVATVEQYA
     PLMAKAPKLF NAIMQPAWMQ TLTEKTIGMI DVPSLSVPTL REELTGHAAL TFSLEQLQAL
     SAEEKARHVL VVQDPFTSFY DAQVVADFVR VAEHLGFKPV LLPFKPNGKP QHVKGFLREF
     ARTAASTAEF LNQLSALDIP MVGVDPALVL CYRDEYREAL GDARGTFEVQ LVQEWLHPRL
     GSVPALSKSS DVWYLLGHCT ESTALPQSSA DWKAIFAHFG AELQAVSVGC CGMAGTYGHE
     AKNRDNSHGI YRLSWQAQLK IRPLNRCLTT GYSCRSQVKR MEKERILHPA QALLSILRSQ
     A
//
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