MENA_ECOLI
ID MENA_ECOLI Reviewed; 308 AA.
AC P32166; Q2M8M6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=1,4-dihydroxy-2-naphthoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01937};
DE Short=DHNA-octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01937};
DE EC=2.5.1.74 {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000269|PubMed:9573170};
GN Name=menA {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000303|PubMed:9573170};
GN Synonyms=yiiW; OrderedLocusNames=b3930, JW3901;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=K12;
RX PubMed=9573170; DOI=10.1128/jb.180.10.2782-2787.1998;
RA Suvarna K., Stevenson D., Meganathan R., Hudspeth M.E.S.;
RT "Menaquinone (vitamin K2) biosynthesis: localization and characterization
RT of the menA gene from Escherichia coli.";
RL J. Bacteriol. 180:2782-2787(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC demethylmenaquinone (DMK). Attaches octaprenylpyrophosphate, a
CC membrane-bound 40-carbon side chain to DHNA. The conversion of DHNA to
CC DMK proceeds in three stages: the removal of the carboxyl group of DHNA
CC as CO(2), the attachment of the isoprenoid side chain, and a quinol-to-
CC quinone oxidation, which is thought to be spontaneous.
CC {ECO:0000269|PubMed:9573170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl
CC diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate;
CC Xref=Rhea:RHEA:26478, Rhea:RHEA-COMP:9563, Rhea:RHEA-COMP:9564,
CC ChEBI:CHEBI:11173, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:55437, ChEBI:CHEBI:58914; EC=2.5.1.74;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01937,
CC ECO:0000269|PubMed:9573170};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000269|PubMed:9573170}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01937, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000305}.
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DR EMBL; U56082; AAB01207.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03062.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76912.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77380.1; -; Genomic_DNA.
DR PIR; S40873; S40873.
DR RefSeq; NP_418365.1; NC_000913.3.
DR RefSeq; WP_000139496.1; NZ_STEB01000017.1.
DR AlphaFoldDB; P32166; -.
DR SMR; P32166; -.
DR BioGRID; 4261778; 7.
DR STRING; 511145.b3930; -.
DR PaxDb; P32166; -.
DR PRIDE; P32166; -.
DR DNASU; 948418; -.
DR EnsemblBacteria; AAC76912; AAC76912; b3930.
DR EnsemblBacteria; BAE77380; BAE77380; BAE77380.
DR GeneID; 66672162; -.
DR GeneID; 948418; -.
DR KEGG; ecj:JW3901; -.
DR KEGG; eco:b3930; -.
DR PATRIC; fig|1411691.4.peg.2775; -.
DR EchoBASE; EB1826; -.
DR eggNOG; COG1575; Bacteria.
DR HOGENOM; CLU_043611_1_1_6; -.
DR InParanoid; P32166; -.
DR OMA; QWIEGAR; -.
DR PhylomeDB; P32166; -.
DR BioCyc; EcoCyc:DMK-MON; -.
DR BioCyc; MetaCyc:DMK-MON; -.
DR BRENDA; 2.5.1.74; 2026.
DR UniPathway; UPA00079; UER00168.
DR PRO; PR:P32166; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate octaprenyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IMP:EcoCyc.
DR GO; GO:0032194; P:ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate; IBA:GO_Central.
DR GO; GO:0042371; P:vitamin K biosynthetic process; IBA:GO_Central.
DR CDD; cd13962; PT_UbiA_UBIAD1; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01937; MenA_1; 1.
DR InterPro; IPR004657; MenA.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR InterPro; IPR026046; UBIAD1.
DR PANTHER; PTHR13929; PTHR13929; 1.
DR Pfam; PF01040; UbiA; 1.
DR PIRSF; PIRSF005355; UBIAD1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Menaquinone biosynthesis;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="1,4-dihydroxy-2-naphthoate octaprenyltransferase"
FT /id="PRO_0000096414"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 42
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 64..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 119..123
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 145..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 170..176
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 198..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 248..250
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 271..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TOPO_DOM 308
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 308 AA; 33594 MW; FECD9E85BAA40E2E CRC64;
MTEQQISRTQ AWLESLRPKT LPLAFAAIIV GTALAWWQGH FDPLVALLAL ITAGLLQILS
NLANDYGDAV KGSDKPDRIG PLRGMQKGVI TQQEMKRALI ITVVLICLSG LALVAVACHT
LADFVGFLIL GGLSIIAAIT YTVGNRPYGY IGLGDISVLV FFGWLSVMGS WYLQAHTLIP
ALILPATACG LLATAVLNIN NLRDINSDRE NGKNTLVVRL GEVNARRYHA CLLMGSLVCL
ALFNLFSLHS LWGWLFLLAA PLLVKQARYV MREMDPVAMR PMLERTVKGA LLTNLLFVLG
IFLSQWAA
