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Database: UniProt
Entry: A0A1Q5MS00_9ACTN
LinkDB: A0A1Q5MS00_9ACTN
Original site: A0A1Q5MS00_9ACTN 
ID   A0A1Q5MS00_9ACTN        Unreviewed;       961 AA.
AC   A0A1Q5MS00;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Dimethylmenaquinone methyltransferase {ECO:0000313|EMBL:OKK16952.1};
GN   ORFNames=AMK16_24650 {ECO:0000313|EMBL:OKK16952.1};
OS   Streptomyces sp. CB00455.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK16952.1, ECO:0000313|Proteomes:UP000185643};
RN   [1] {ECO:0000313|EMBL:OKK16952.1, ECO:0000313|Proteomes:UP000185643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00455 {ECO:0000313|EMBL:OKK16952.1,
RC   ECO:0000313|Proteomes:UP000185643};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKK16952.1}.
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DR   EMBL; LIVQ01000006; OKK16952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5MS00; -.
DR   STRING; 1703927.AMK16_24650; -.
DR   Proteomes; UP000185643; 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   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; 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; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:OKK16952.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185643};
KW   Transferase {ECO:0000313|EMBL:OKK16952.1}.
FT   DOMAIN          39..254
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          678..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   961 AA;  100157 MW;  9E5187AA58B8CDD9 CRC64;
     MDAVTSPGEL ERTLRAELRG EVDFGAAARA LVTMDASNYR RVPLGVVAPR DAEDVAAALR
     VCAAAGVPVV PRGGGTSIAG QATGTGVVLD FTRHMNAVLS VDPAARTAVV QPGLVLDRLR
     DAVRPYGLTF GPDPSTRSRC TLGGMIGNNA CGAHSVAWGT TADNVAELAV AAYGGAAHRI
     STGWAGAPAG LSELVDGHLG LLRTGMPPEF SRRISGYDLQ SLLPERGVRL ARAFCGSEGT
     LGVVTEAVVR LVEAPRAPVL AVLGYADETA AADAAAGLLP YGPLTVEGMA RDLVGDAAGL
     PRGGAWLFVE MPDAGAALPL VRGADALDAL VVADPARQRA LWRIREDAAG TATRMPGGAA
     GAGPGAESGA GAMAWPGWED CAVPPARLGA YLRAFRALLA EHGLHGSPYG HFGEGCVHVR
     IDFDLVTREG VARFRTFSQE LAALVVDHGG SLSGEHGDGQ ARAELLPRMY GARVVRLFGA
     YKDVWDPAGG MNPGILARPA RLDENLRFAV LPRTPFAQDV ARCVGVAKCR SHESGTAAVM
     CPSYRVTGEE RHSTRGRARL LHEMLAGEVV TDGWRSSEVA GALDLCLGCK GCLSDCPVGV
     DMAAHKAEFL HRHWAGRLRP LAHYTLGGLP AWLHLIARLR AARPVNALAR LFPAPGLTRE
     RPLPQLAREP FSHWWRTRPA APGPSVPGRV SGGAGAADRA GAVGPGEAAG RGPGEAAVLG
     SGPAAGNAPV VTLWPDTFTE YLAPEAGRAA VRVLEDAGLR VAVPRGPVCC GLTYVSTGRL
     DRARTVLRRT LDAVDAQAGT PGPVLVLEPS CAAALRGDLP ALLPDDPRAR RLASAVRTFA
     ETLEEYAPQW RPPRLDRSVA GQTHCHQHAV LGDAADRRLR ERAGLVGDLS GGCCGLAGNF
     GFEPGHHEVS VACAEEQLLP SLRAAPGDAL VQADGYSCRT QIAQLGGVRA RHLAEILADG
     L
//
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