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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//