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Database: UniProt
Entry: A0A0J1CW84_9BURK
LinkDB: A0A0J1CW84_9BURK
Original site: A0A0J1CW84_9BURK 
ID   A0A0J1CW84_9BURK        Unreviewed;       960 AA.
AC   A0A0J1CW84;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Dimethylmenaquinone methyltransferase {ECO:0000313|EMBL:KLU24591.1};
GN   ORFNames=EOS_19325 {ECO:0000313|EMBL:KLU24591.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU24591.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU24591.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
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:KLU24591.1}.
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DR   EMBL; AEJF01000122; KLU24591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1CW84; -.
DR   PATRIC; fig|908627.4.peg.4327; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
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   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; 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; IPR004017; Cys_rich_dom.
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   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; PF02754; CCG; 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   Methyltransferase {ECO:0000313|EMBL:KLU24591.1};
KW   Transferase {ECO:0000313|EMBL:KLU24591.1}.
FT   DOMAIN          26..254
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   960 AA;  106017 MW;  4093AB6564B72777 CRC64;
     MRAALGPAVR FDAAHRAAYA SDASNYRQTP IGVVVPASID ELIAAVAICR HHNVPILSRG
     GGTSMSGQTV NVAVVFDLSK SCNRILDVNE TQRTALVEPG VICDTLRDAA EVYGLTFAPD
     PSTHSRCTLG GMIGNNSCGP HSVMAGKTLE NVEALEVMTY DGERFWVGPT FDDELEAIIA
     AGGRRGQIYS DLKDLRDRYA TQIRTRFPDI RRRVSGFNLD QLLPENGFNV ARALVGTEGT
     CALTVAAKVR LVPSPAVRVS LVLGFPDIYA AADALPEYRQ FKPIAIEGLD REIIRGLQAR
     GLRAGEIAML PAGDAWVIVE FGADTVEQAV ALAEQTVLSL AARTTGPIPS TWLVTDPDMQ
     KRIWLIRETG ASATQLSIDP TVPDPKVGWE DVAVDPDQLG DYLRAFQALV ERYGYRTSLF
     GHFGDGCVHA RITFDLTSAA GVSQWRNFTR EAAELVVRYG GSLSGEHGDG QAKAEFLPIM
     FGEELMEAMR EFKRIWDPQN RMNPGKVVQA YRLDDNLRMG PQYKVVNFHT RFAFRSAEGN
     GFQRAVERCV GMGRCRSLTG STMCPSYRAT REERYSTRGR SRLLWEMLQG DVVDGQWNSE
     PVKEALDTCL SCKGCRSDCP THVDMATYKA EFLSHYYETK RRPRQALFMG RIGDWAPLAA
     KWPWMANLLT QTPAFATLAK RIAGTAQRRA LPRFASQTFR TRFAEDRSNN TLNKSAAPLR
     GKVILWVDTF CEHFHPEIAL AAVKVLRHAG FETVLPAKLL CCGRPLYDFG YLDTAREKLE
     AILTTLALEF ARDDPGDVPL ALVGLEPGCM SVFKDELLKL FPDDPRAQRL ASSVWLFGDF
     LVEQNYVPPR FEAQVLVHAH CHQKSLFGTN GERVLLERMG ARFTLLDSGC CGLAGSFGFH
     PDHIDIADNV GEQVLFPAVR QASKDTIVLT NGFSCREQIR HGTRREAMHL AELLALACGA
//
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