ID I0GXF4_ACTM4 Unreviewed; 413 AA.
AC I0GXF4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Cyclic dehypoxanthine futalosine synthase {ECO:0000256|HAMAP-Rule:MF_00992};
DE Short=Cyclic DHFL synthase {ECO:0000256|HAMAP-Rule:MF_00992};
DE EC=1.21.98.1 {ECO:0000256|HAMAP-Rule:MF_00992};
DE AltName: Full=Dehypoxanthine futalosine cyclase {ECO:0000256|HAMAP-Rule:MF_00992};
DE Short=DHFL cyclase {ECO:0000256|HAMAP-Rule:MF_00992};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnC {ECO:0000256|HAMAP-Rule:MF_00992};
GN Name=mqnC {ECO:0000256|HAMAP-Rule:MF_00992};
GN OrderedLocusNames=AMIS_2210 {ECO:0000313|EMBL:BAL85441.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL85441.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL85441.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Radical SAM enzyme that catalyzes the cyclization of
CC dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine
CC (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehypoxanthine futalosine + S-adenosyl-L-methionine = 5'-
CC deoxyadenosine + cyclic dehypoxanthinylfutalosinate + H(+) + L-
CC methionine; Xref=Rhea:RHEA:33083, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:58864,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64270; EC=1.21.98.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00992};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00992};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|HAMAP-Rule:MF_00992};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnC family.
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
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; AP012319; BAL85441.1; -; Genomic_DNA.
DR RefSeq; WP_014440341.1; NC_017093.1.
DR AlphaFoldDB; I0GXF4; -.
DR STRING; 512565.AMIS_2210; -.
DR KEGG; ams:AMIS_2210; -.
DR PATRIC; fig|512565.3.peg.226; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_1_0_11; -.
DR OMA; ATMMFGS; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000007882; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046992; F:oxidoreductase activity, acting on X-H and Y-H to form an X-Y bond; IEA:UniProtKB-UniRule.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00992; MqnC; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR022431; Cyclic_DHFL_synthase_mqnC.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00423; CofH family radical SAM protein; 1.
DR NCBIfam; TIGR03699; menaquin_MqnC; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004762; CHP00423; 2.
DR SFLD; SFLDF00342; cyclic_dehypoxanthine_futalosi; 1.
DR SFLD; SFLDG01064; F420__menaquinone_cofactor_bio; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00992};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00992};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00992}; Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00992};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00992}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00992};
KW Reference proteome {ECO:0000313|Proteomes:UP000007882};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00992}.
FT DOMAIN 54..301
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00992"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00992"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00992"
SQ SEQUENCE 413 AA; 45430 MW; 0A8A8F8691D8D3F4 CRC64;
MTANPEIDSI LQRGADGGRI TPEEALLLYT QAPFHALGEA ADAVRRRRYP DGIVTYLIDR
NINYTNVCVT ACKFCAFFRA PKHKEGWSHP TEEILRRCGE AVDLGATQVM LQGGHHPDYG
VAYYEDLFSS VKQAYPQLAI HSIGPSEILH MAKVDGVSIE EAVIRIKAAG LDSIAGAGAE
MLPERPRKAI APLKESGERW LEVMAVAHRH GLSSTATMMM GTGETNAERI EHITMIRGVQ
DLAVANGYRD DAVEKDHTVG GFRAFIPWTY QPENNHLKGR TQATTVEYLR FIAVSRLFFD
NVAHLQASWL TTGKDIGQLS LHMGVDDLGS IMLEENVISS AGARHRSNLQ GLISMIRTAD
RIPAQRDTWY RHLAVHRTAA EDPTDERVVS HFSSIAIKGG GAGRTQLPLV DAS
//