ID A0A014N9J7_9GAMM Unreviewed; 481 AA.
AC A0A014N9J7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=FAD-binding molybdopterin dehydrogenase {ECO:0000313|EMBL:EXU76078.1};
GN ORFNames=BG55_07565 {ECO:0000313|EMBL:EXU76078.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU76078.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU76078.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU76078.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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:EXU76078.1}.
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DR EMBL; JFHN01000037; EXU76078.1; -; Genomic_DNA.
DR RefSeq; WP_034935940.1; NZ_JFHN01000037.1.
DR AlphaFoldDB; A0A014N9J7; -.
DR STRING; 69222.BG55_07565; -.
DR PATRIC; fig|69222.5.peg.1550; -.
DR OrthoDB; 9775084at2; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 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; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
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 InterPro; IPR012175; Xanth_DH_ssu_bac.
DR InterPro; IPR014307; Xanthine_DH_ssu.
DR NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR PANTHER; PTHR45444:SF3; ALDEHYDE OXIDASE_XANTHINE DEHYDROGENASE, MOLYBDOPTERIN BINDING PROTEIN; 1.
DR PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF036557; XdhA_RC; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019918}.
FT DOMAIN 1..85
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 187..360
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 481 AA; 52905 MW; 06C6780FE807BC77 CRC64;
MIQFLLNQTL VSEASLDPNL TVLNYLRQNK RRCGTKEGCA SGDCGACTVT LGRVENDAMV
WETVNSCMTF VSALQGKQLI TVEDLKQGDK LHPVQQAMVD CHASQCGFCT PGFVMSLFTL
QKNSDGWQHK QAEQALAGNL CRCTGYRPIV DAARQACQQP EQDSFRQQEA ATVARLLALK
NDQVQEMALN GNRCLLPKTP TQLAELLTAH PQAKLLAGGT DLALEVTQRH HALPLMIALG
QIEELKQCYV SDDEIILGAG ASLHFCQAFL QQHIPQFAAL LDRFASLQIR NQGTLGGNIA
NGSPIGDTPP LLLALNATLE LQQGESLRRL PLSDFFLSYR KTALRQGEFI RAVRIKKVTS
SQNLRVWKVS KRYEDDISAV CAAMLLETDG DGVVREARVA FGGMAEIPKR ATHCEQQLVG
KPLTQSSVER ACSALSQDFR PLSDLRASAD YRLQVAKNLL RRYHAALGDQ LSLLEVTDYV
P
//
