ID B4UAZ3_ANASK Unreviewed; 626 AA.
AC B4UAZ3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00992, ECO:0000256|HAMAP-Rule:MF_00995};
DE Includes:
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 AltName: Full=Menaquinone biosynthetic enzyme MqnC {ECO:0000256|HAMAP-Rule:MF_00992};
DE Short=DHFL cyclase {ECO:0000256|HAMAP-Rule:MF_00992};
DE Includes:
DE RecName: Full=Chorismate dehydratase {ECO:0000256|HAMAP-Rule:MF_00995};
DE EC=4.2.1.151 {ECO:0000256|HAMAP-Rule:MF_00995};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnA {ECO:0000256|HAMAP-Rule:MF_00995};
GN Name=mqnC {ECO:0000256|HAMAP-Rule:MF_00992};
GN Synonyms=mqnA {ECO:0000256|HAMAP-Rule:MF_00995};
GN OrderedLocusNames=AnaeK_0399 {ECO:0000313|EMBL:ACG71641.1};
OS Anaeromyxobacter sp. (strain K).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG71641.1, ECO:0000313|Proteomes:UP000001871};
RN [1] {ECO:0000313|EMBL:ACG71641.1, ECO:0000313|Proteomes:UP000001871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|EMBL:ACG71641.1,
RC ECO:0000313|Proteomes:UP000001871};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA Beliaev A.;
RT "Complete sequence of Anaeromyxobacter sp. K.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of chorismate into 3-[(1-
CC carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone
CC (MK, vitamin K2). {ECO:0000256|HAMAP-Rule:MF_00995}.
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=chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O;
CC Xref=Rhea:RHEA:40051, ChEBI:CHEBI:15377, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:76981; EC=4.2.1.151; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00995};
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|ARBA:ARBA00004863, ECO:0000256|HAMAP-Rule:MF_00992}.
CC -!- SIMILARITY: Belongs to the MqnA/MqnD family. MqnA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00995}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnC family.
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
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DR EMBL; CP001131; ACG71641.1; -; Genomic_DNA.
DR RefSeq; WP_012524474.1; NC_011145.1.
DR AlphaFoldDB; B4UAZ3; -.
DR KEGG; ank:AnaeK_0399; -.
DR HOGENOM; CLU_029835_0_0_7; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001871; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
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; cd13634; PBP2_Sco4506; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR HAMAP; MF_00995; MqnA; 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; IPR003773; Menaquinone_biosynth.
DR InterPro; IPR030868; MqnA.
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 Pfam; PF02621; VitK2_biosynth; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDF00342; cyclic_dehypoxanthine_futalosi; 1.
DR SFLD; SFLDG01064; F420__menaquinone_cofactor_bio; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {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};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00995};
KW 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00992}.
FT DOMAIN 319..549
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 333
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 337
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 340
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 626 AA; 68809 MW; BBAF39AEA05EE7F2 CRC64;
MPKKIRAAAV SFLNAWPLTA GLEGSERIEL VLAEPSRCAA MLEAGEVDLA LVSVAALTKG
QYDIVPGIAI GADGPVQTVV LAGEQSPAIW DEVFLDTASR TSHVLAKLVL DAMGVHPRFT
PMHADEGLAR ARGTKGALVI GDRGFGVRAN HVLDLGREWT RLTGLPMIFA LWAARPGAVT
PEDVQELTRA AQHGLGIRTE LAQKFAAQKG GDPEKYRRYL TQKIRYGLGP YELQGLEAFL
ERAAAKGFLP PMPLRFVDDV VRTRRVRRAV SVDTALQKGA DGERLDADEA ATLDEKAPLL
ELGLAADQRR RALHPGDLVT YIVSRNVNYT NVCTTACHFC AFYRPRGHQE SYVLTREELT
QKIDETVALG GIEILLQGGL HPDLGVEWYE DLFRWVKQTW PVINLHALSP EEIWHIARTS
ELGLEATIDR LVAAGMDSIP GGGAEILDDE VRRRIAPLKC STDEWLTVMK AAHLKGLKST
ATMMFGVGEG PEHRVAHLMR LRELQDETHG FTAFICWPFQ SQNTRLEPGD GSAHAYLRTN
ALSRLVLDNV PNLQASWVTM GGGVAQAALH MGCNDFGQVM IEENVVSAAG TTFKMDSEEV
ERHIRDAGFR AARRNMKYQL VEETRA
//
