MQNC_ALKHC
ID MQNC_ALKHC Reviewed; 370 AA.
AC Q9K864;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cyclic dehypoxanthine futalosine synthase {ECO:0000255|HAMAP-Rule:MF_00992};
DE Short=Cyclic DHFL synthase {ECO:0000255|HAMAP-Rule:MF_00992};
DE EC=1.21.98.1 {ECO:0000255|HAMAP-Rule:MF_00992, ECO:0000269|PubMed:23763543};
DE AltName: Full=Dehypoxanthine futalosine cyclase {ECO:0000255|HAMAP-Rule:MF_00992};
DE Short=DHFL cyclase {ECO:0000255|HAMAP-Rule:MF_00992};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnC {ECO:0000255|HAMAP-Rule:MF_00992};
GN Name=mqnC {ECO:0000255|HAMAP-Rule:MF_00992}; OrderedLocusNames=BH3143;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND REACTION MECHANISM.
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=23763543; DOI=10.1021/bi400498d;
RA Cooper L.E., Fedoseyenko D., Abdelwahed S.H., Kim S.H., Dairi T.,
RA Begley T.P.;
RT "In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC
RT involved in the biosynthesis of futalosine-derived menaquinone.";
RL Biochemistry 52:4592-4594(2013).
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:0000255|HAMAP-Rule:MF_00992, ECO:0000269|PubMed:23763543}.
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:0000255|HAMAP-Rule:MF_00992,
CC ECO:0000269|PubMed:23763543};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:23763543};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is likely coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:23763543};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00992}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnC family.
CC {ECO:0000255|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; BA000004; BAB06862.1; -; Genomic_DNA.
DR PIR; G84042; G84042.
DR RefSeq; WP_010899286.1; NC_002570.2.
DR AlphaFoldDB; Q9K864; -.
DR SMR; Q9K864; -.
DR STRING; 272558.10175765; -.
DR EnsemblBacteria; BAB06862; BAB06862; BAB06862.
DR KEGG; bha:BH3143; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_1_0_9; -.
DR OMA; ATMMFGS; -.
DR OrthoDB; 419725at2; -.
DR BioCyc; MetaCyc:MON-18222; -.
DR BRENDA; 1.21.98.1; 661.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001258; 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 Gene3D; 3.20.20.70; -; 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; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03699; menaquin_MqnC; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Menaquinone biosynthesis; Metal-binding;
KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..370
FT /note="Cyclic dehypoxanthine futalosine synthase"
FT /id="PRO_0000425603"
FT DOMAIN 50..295
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00992"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00992"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00992"
SQ SEQUENCE 370 AA; 42074 MW; D76BAB15E30B4411 CRC64;
MSIDGILERA VNGERLSMED AVKLYESDEV EKMGAAANQI MLKWHPEPIT TFVIGRNVNY
TNFCDTYCRF CAFYRAPGHK EGYVLDDEVI LKKIQETIDV GGTEILMQGG TNPDLTIDYY
TDLLRNIKER FPNIWMHSFS PAEVWKIAEV SSMSVEEVLR ELHEAGLDSM PGGGAEILTE
ETRLRVSRLK ITWEQWINAM KATKKVGMHG TATMVIGFGE SFEERALHLQ RVRDAQDETE
CFTAFISWLF QPENTGMYKT KKLTPRDYLK NVAISRLFLD NIPNFQSSWV TMGPEVGKLS
LQYGCNDFGS TMIEENVVSA AGTTHKVNTN KILQLIREAG KIPAQRTTSY EIIRTFEDKE
AAEKDFVMQN
