ID A0A0T1Q2D0_9ACTN Unreviewed; 926 AA.
AC A0A0T1Q2D0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dimethylmenaquinone methyltransferase {ECO:0000313|EMBL:KQX10636.1};
GN ORFNames=ASC82_23545 {ECO:0000313|EMBL:KQX10636.1};
OS Streptomyces sp. Root431.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736535 {ECO:0000313|EMBL:KQX10636.1, ECO:0000313|Proteomes:UP000051818};
RN [1] {ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|Proteomes:UP000051818};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX10636.1, ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|EMBL:KQX10636.1,
RC ECO:0000313|Proteomes:UP000051818};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX10636.1}.
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DR EMBL; LMEI01000012; KQX10636.1; -; Genomic_DNA.
DR RefSeq; WP_056651784.1; NZ_LMEI01000012.1.
DR AlphaFoldDB; A0A0T1Q2D0; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000051818; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
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; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:KQX10636.1};
KW Transferase {ECO:0000313|EMBL:KQX10636.1}.
FT DOMAIN 50..266
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 926 AA; 97306 MW; 142CB299271FB451 CRC64;
MRRGLRHPGV VGTHEDHASA LAAELRAAVA GDVDFSVTAR ALTTMDASNY RRVPVGTVAP
RDAADVAAVL EVCRAHGTTP VVARGGGTSI GGQATGTGVV LDLTRHMAGL VSLDPEERTA
VVRPGLVLDR LREAARPYGL TFGPDPSTHS RCTLGGMIGN NACGAHSVAW GTTADNVRSL
DVVTYGGERL TLGRDGRGAP AGLLDLVGRN LALLRTGYPA GLPRRISGYA LDALLPEKGV
DVVRSFCGSE GTLGVVTEAT VRLVPLPADP VLVVLGYPDE SAAAEAAAGL LPYGPLTVEG
MAADLVRGGA GAGGLPRGGA WLFVETDGPS AAAGLVRAAD ALDSVVVRDP AGQRALWRIR
EDAAGTATRL PGGGEAWPGW EDCAVPPARL GAYLREFRAL LADFGLRGIP YGHFGDGCVH
VRIDFDLWTK KGVRDFRRFS EAVADLVVAH GGSLSGEHGD GQARAELLPR MYGEELVGLF
GAVKDVWDPD GGLNPGMLVR PKPLDSGLRF EGLPLVGVGR EAARCVGVAK CRVEGPSSGA
TVMCPSYRAT GEEKHSTRGR ARLLHEMALG EVITDGWRSE EVREALDLCL SCKGCRSDCP
VGVDMAAYKA EFLDRHYAGP LGLLRRPRSH WTMGGLPRWL ALFGRGVNAA TRLPFAARLA
GVTPERSMPR VADRTFVSWF GERGSRRPPT LTLWPDTFTN HLSPEVGRAA VRVLEDAGLG
VALPPGRVCC GLTYVSTGRL GAARKAMRRT LDVLGLSAAP GPVVVLEPSC AATLRTDLPE
LLPDDPRAAR LAASVLTFAE ALETLAPDWT PPRLDRPVAG QTHCHQHAVL GDAPDRRLRA
HAGLTGELSG GCCGLAGNFG FEPAHYEVSV ACAEDQLLPA LRAAPEGSEV LADGFSCRTQ
IADLAGGRAR HLAEVLAEGL EEGQER
//