ID D2UGK2_XANAP Unreviewed; 327 AA.
AC D2UGK2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Probable vanillate o-demethylase oxidoreductase (Ferredoxin like protein) {ECO:0000313|EMBL:CBA17513.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:CBA17513.1};
GN Name=vanB {ECO:0000313|EMBL:CBA17513.1};
GN OrderedLocusNames=XALc_3036 {ECO:0000313|EMBL:CBA17513.1};
OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA17513.1, ECO:0000313|Proteomes:UP000001890};
RN [1] {ECO:0000313|EMBL:CBA17513.1, ECO:0000313|Proteomes:UP000001890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA Rott P.;
RT "The complete genome sequence of Xanthomonas albilineans provides new
RT insights into the reductive genome evolution of the xylem-limited
RT Xanthomonadaceae.";
RL BMC Genomics 10:616-616(2009).
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DR EMBL; FP565176; CBA17513.1; -; Genomic_DNA.
DR RefSeq; WP_012917506.1; NC_013722.1.
DR AlphaFoldDB; D2UGK2; -.
DR STRING; 380358.XALC_3036; -.
DR GeneID; 57878346; -.
DR KEGG; xal:XALC_3036; -.
DR PATRIC; fig|29447.3.peg.3003; -.
DR eggNOG; COG1018; Bacteria.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000001890; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF2; PHENOXYBENZOATE DIOXYGENASE BETA SUBUNIT; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Methyltransferase {ECO:0000313|EMBL:CBA17513.1};
KW Oxidoreductase {ECO:0000313|EMBL:CBA17513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW Transferase {ECO:0000313|EMBL:CBA17513.1}.
FT DOMAIN 5..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..324
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 327 AA; 35635 MW; AB7A3F35BD82B6BE CRC64;
MRKDSQWNTA RIVAVTTPCQ EVREIEFDPG SAGRHFTVGS HIDVRVHIGD TPDVRSYSLV
GEPAADGHYR IAVRAVAGSR GGSRAMWALA VGDQVEISAP NNQFALDENA EHIVLIAGGI
GITPILGMAQ RLARSPLPFQ LLYAGRSQAT MAYLEPLQAL LGERLKVFCP EHLGRLELAT
QIAQWPRGAD VYACGPLPLL DELRQRWRED GRARARLHFE TFGNSGHAPA QGFEVEIPTL
GKTVQVGAHQ SLLDALSAAG VEVMADCQRG ECGLCVVDVL DSTSPLDHRD VFLSEEQHRD
NRKLCACVSR ALGGRIRIDT GYRADAF
//