ID A0A0M8QRG6_9ACTN Unreviewed; 1023 AA.
AC A0A0M8QRG6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dimethylmenaquinone methyltransferase {ECO:0000313|EMBL:KOT40506.1};
GN ORFNames=ADK41_12050 {ECO:0000313|EMBL:KOT40506.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT40506.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT40506.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT40506.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOT40506.1}.
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DR EMBL; LGCN01000120; KOT40506.1; -; Genomic_DNA.
DR RefSeq; WP_030824104.1; NZ_LGCN01000120.1.
DR AlphaFoldDB; A0A0M8QRG6; -.
DR PATRIC; fig|36816.3.peg.2598; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000037773; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KOT40506.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037773};
KW Transferase {ECO:0000313|EMBL:KOT40506.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 990..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..280
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1023 AA; 112225 MW; D87CC2A4925B4DEA CRC64;
MEPVDLPLPV VRRPRASIDA RALERDLRAR VDGEVRFDAG TRAAYSTDGS NYRQVPIGVV
VPRTVEAAVE AVAVCRGHGA PLLSRGGGTS LAGQCCNTAV VLDWSKYGNR LLSVDPDGRR
CVVEPGIVLD DLNRRLAGYG LQYGPRPATH PNCTIGGMIG NNSCGSTAQA YGKVVDNLHR
LEVLTHDGVR MWVGRTDEGE LERLTASDGR TGELYRGLVA LRDRYAGLVR ERYPDIPRRV
SGYNLDSLLP EHGFDVAGLL TGSESTLVTV LRAELELVPV PKHTALVVLG YEDICRAADH
VPAVLEHEPV ALEGVDHQLI HFQRIKHLNP EALGELPRGR AYLMVQLAGD TREEADARAR
ALIDAKPDDV DHTWYDDERH VHELWLVRES GLGATAHVPG EPDTWEGWED SAVPVDRLGD
YLRDLKRLYE EFDYGHPSVY GHFGHGCVHT RTPFDLESEE GVARMRAFVE RAADLVVSYG
GSLSGEHGDG QSRGELLERM FGPELIEGFE RLKGLFDPDN RMNPGKIVLP YRLDENLRLG
ADHLPWEPET VFSFPHDEGR FSRAATRCVG VGKCRSLEGG VMCPSYRATR EEEHSTRGRA
RLLFEMVDND GDSPITDGWR SDEVHDALDL CLACKGCKTD CPVNVDMATY KAEFLHHHYK
GRPRPLAHYS MGWLPALARV VALAPRTVNA WASVPWVARA AKALGGVAPE RDVPVFAEQR
FTDWWRERGG PRGEGHRGEV VVWPDTFTDH FHPAIGRAAV EVLEAAGFRV KVPRAAVCCG
LTWISTGQLN VARRVLGHTI DVLREDLRRG TPVIGLEPSC TAVFRADAAE LLPKDPDVGR
LREQTRTLAE LLLERAGDWP PPRVDARAVV QRHCHQYAVM GFDADREILR RAGVDADVLD
AGCCGLAGNF GFEKGHYEVS MACAEAGLLP AVRDADDATL VLADGFSCRT QVDQAGTGRT
PLHLAEVLAA GLTGREAAPE RPEAPGPRAL LPWGVAGTAA GALAVSAVVR RLRRTRRPGR
PPR
//
