(data stored in SCRATCH zone)

SWISSPROT: Q2IMW4_ANADE

ID   Q2IMW4_ANADE            Unreviewed;       626 AA.
AC   Q2IMW4;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=Adeh_0371 {ECO:0000313|EMBL:ABC80147.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80147.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC80147.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC80147.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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
CC       menaquinone (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
CC       futalosine (CDHFL), a step in the biosynthesis of menaquinone (MK,
CC       vitamin K2). {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|HAMAP-Rule:MF_00995}.
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; CP000251; ABC80147.1; -; Genomic_DNA.
DR   RefSeq; WP_011419430.1; NC_007760.1.
DR   STRING; 290397.Adeh_0371; -.
DR   EnsemblBacteria; ABC80147; ABC80147; Adeh_0371.
DR   KEGG; ade:Adeh_0371; -.
DR   eggNOG; ENOG4105DKF; Bacteria.
DR   eggNOG; COG1060; LUCA.
DR   eggNOG; COG1427; LUCA.
DR   HOGENOM; HOG000003657; -.
DR   KO; K11784; -.
DR   OMA; IWHIART; -.
DR   BioCyc; ADEH290397:G1G5W-381-MONOMER; -.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000001935; 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   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00995; MqnA; 1.
DR   HAMAP; MF_00992; MqnC; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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   PANTHER; PTHR43076; PTHR43076; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF02621; VitK2_biosynth; 1.
DR   SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR03699; menaquin_MqnC; 1.
DR   TIGRFAMs; TIGR00423; TIGR00423; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMW4.
DR   SWISS-2DPAGE; Q2IMW4.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00992};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00992};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00992};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00995};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00995};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00992};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00992};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00992}.
FT   DOMAIN      328    497       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   METAL       333    333       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00992}.
FT   METAL       337    337       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00992}.
FT   METAL       340    340       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00992}.
SQ   SEQUENCE   626 AA;  68749 MW;  669DE23AE6FB4924 CRC64;
     MPKKIRAAAV SFLNAWPLTA GLEGSERIEL VQAEPSRCAA MLEAGEVDLA LVSVAALTKG
     QYDIVPGIAI GADGPVQTVV LAGEQSPAIW DEVFLDTASR TSHVLAKLVL DAKGVHPRFT
     PMPAEEGLAR AKGTKGALVI GDRGFGVRAN HVLDLGREWT QLTGLPMIFA LWAARPGAVS
     PEDVQELTRA AQHGLGIRTE LAQKFAALKG GDPEKYRRYL TQKIRYGLGP YELQGLEAFL
     ERAATKGFLP PMPLRFVDDV VRTRRVRRAV SVDTALQKGA DGERLDADEA ATLDEHAPLL
     ELGLAADARR RALHPGDLVT YIVSRNVNYT NVCTTACHFC AFYRPRGHQE SYVLTREELT
     QKIDETVALG GIEILLQGGL HPDLGVEWYE DLFRWVKQTW PVINLHALSP EEIWHIARTS
     ELGLEATIDR LIAAGMDSIP GGGAEILDDE VRRRIAPLKC STDEWLTVMK AAHRKGLKST
     ATMMFGVGEG PEHRVAHLMR LRELQDETHG FTAFICWPFQ SQNTRLEPGD GSAHAYLRTN
     ALSRLVLDNV PNLQASWVTM GGGVAQAALH MGCNDFGQVM IEENVVSAAG TTFKMDSEEV
     ERHIRDAGFR AARRNMKYQL VEETRA
//

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