ID   D3V1T8_XENBS            Unreviewed;      1023 AA.
AC   D3V1T8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Putative oxidase, with FAD-binding domains {ECO:0000313|EMBL:CBJ81632.1};
GN   Name=ydiJ {ECO:0000313|EMBL:CBJ81632.1};
GN   OrderedLocusNames=XBJ1_2508 {ECO:0000313|EMBL:CBJ81632.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ81632.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ81632.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ81632.1};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA   Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA   Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA   Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA   Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA   Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA   Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA   van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA   Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA   Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT   convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:E27909-E27909(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FN667741; CBJ81632.1; -; Genomic_DNA.
DR   RefSeq; WP_012988936.1; NC_013892.1.
DR   AlphaFoldDB; D3V1T8; -.
DR   STRING; 406818.XBJ1_2508; -.
DR   KEGG; xbo:XBJ1_2508; -.
DR   PATRIC; fig|406818.4.peg.2258; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_1_0_6; -.
DR   Proteomes; UP000002045; Chromosome.
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; -; 2.
DR   Gene3D; 3.30.70.2740; -; 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; 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: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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          48..281
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1023 AA;  114980 MW;  5ECEDD764887F9EB CRC64;
     MIPRIPQAPH VSELAQEYLT ALKEVGFTGD TVSSYADRLT MATDNSIYQL LPQAVIFPRS
     SADVALLARV AGEERFYSLT FTPRGGGTGT NGQSLNNGIV VDMSRYMNRI LEINPEQGWV
     KVEAGVIKDQ LNQYLKPFGY FFSPELSTSN RATLGGMINT DASGQGSLVY GKTSDHVLGV
     RAVLLGGEMF DTRPMSTLFA ESIAQEESVI GQIYKTVLER CREQRKLIVE KFPKLNRFLT
     GYDLRHVYSD DMQTFDLTRI LTGSEGTLAF ITEATLDITP LPKVRRLVNA KYDSFDSALR
     NAPFMVEAKA LSVETVDSTV LNLAREDIIW HSVKELITDV ADKDMQGLNI VEFSGNDEQQ
     IDQQVYDLCQ RLDELMEENQ TGIIGYQICH HLVDIERIYA MRKKSVGLLG NSKGNAKPIP
     FVEDTCVPPQ HLADFITEFR QLLDSHQLNY GMFGHVDAGV LHVRPALDMC DPQQEILMKQ
     ISDEIVRLTA KYGGLLWGEH GKGFRAEYSP DFFGDILYDE LRRIKAAFDP LNRLNPGKIC
     SPIDTDAPMM KVDAAKRGTY DRTIPVNVRT AFRGAMECNG NGLCFNFDVK SPMCPSMKVS
     QHRIHSPKGR ATLVREWLRL LTEQGVNPKL LEQGLDQAHP SLRGLIDKTR YSWQAWRGEY
     DFSHEVKEAM SGCLACKACS TQCPIKIDVP SFRSSFLSLY HSRYLRPLRD HIVANVESST
     PLMAKVPQVF NFFLKQPWVQ KISQHTIGMV DLPLLSYPTL QQQLSGHYAA RTTLEQLETL
     SQSQRKQHVL IVQDPFTSYH DAKVVADFVR LTEKLGYQPV LLPFSPNGKA QHVKGFLTKF
     AKTAEKTASF LNRIACLNIP MVGIDPALVL CYRDEYKDIL GERRGNFSVQ LVHEWLMDIL
     PETPAQEKRD DSTSSYDWYL LGHCTEVTAL PNSGKQWTDI FRHFGCQLNN VSVGCCGMAG
     TYGHEKKNID NSIGIYKLSW APALGNLGLE RCLSTGYSCR SQVKRMEGQT VKHPLQALLE
     IIP
//