MENA_MYCTU
ID MENA_MYCTU Reviewed; 292 AA.
AC P9WIP3; L0T6Z2; O06400; P65650;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
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:30978223};
DE AltName: Full=Isoprenyl diphosphate:1,4-dihydroxy-2-naphthoate isoprenyltransferase {ECO:0000303|PubMed:30978223};
GN Name=menA {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000303|PubMed:30978223};
GN OrderedLocusNames=Rv0534c; ORFNames=MTCY25D10.13c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=30978223; DOI=10.1371/journal.pone.0214958;
RA Dhiman R.K., Pujari V., Kincaid J.M., Ikeh M.A., Parish T., Crick D.C.;
RT "Characterization of MenA (isoprenyl diphosphate:1,4-dihydroxy-2-naphthoate
RT isoprenyltransferase) from Mycobacterium tuberculosis.";
RL PLoS ONE 14:E0214958-E0214958(2019).
CC -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC demethylmenaquinone (DMK). Can use a variety of allylic isoprenyl
CC diphosphates as substrates but has a requirement for at least three
CC isoprene units. {ECO:0000269|PubMed:30978223}.
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:30978223};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30978223};
CC Note=Can also use Fe(2+) or Zn(2+), with lower efficiency.
CC {ECO:0000269|PubMed:30978223};
CC -!- ACTIVITY REGULATION: Activity is abolished by EDTA. Inhibited by Ro 48-
CC 8071, which is non-competitive with regard to DHNA and competitive with
CC regard to the isoprenyldiphosphate substrate.
CC {ECO:0000269|PubMed:30978223}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.2 uM for DHNA {ECO:0000269|PubMed:30978223};
CC KM=4.3 uM for farnesyl diphosphate {ECO:0000269|PubMed:30978223};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:30978223};
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:0000305|PubMed:30978223}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01937,
CC ECO:0000269|PubMed:30978223}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01937}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:30978223}.
CC -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01937}.
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DR EMBL; AL123456; CCP43272.1; -; Genomic_DNA.
DR PIR; A70546; A70546.
DR RefSeq; NP_215048.1; NC_000962.3.
DR RefSeq; WP_003402865.1; NZ_NVQJ01000036.1.
DR AlphaFoldDB; P9WIP3; -.
DR SMR; P9WIP3; -.
DR STRING; 83332.Rv0534c; -.
DR PaxDb; P9WIP3; -.
DR DNASU; 887408; -.
DR GeneID; 45424498; -.
DR GeneID; 887408; -.
DR KEGG; mtu:Rv0534c; -.
DR TubercuList; Rv0534c; -.
DR eggNOG; COG1575; Bacteria.
DR OMA; QWIEGAR; -.
DR PhylomeDB; P9WIP3; -.
DR UniPathway; UPA00079; UER00168.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate octaprenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IBA:GO_Central.
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 HAMAP; MF_01937; MenA_1; 1.
DR InterPro; IPR004657; MenA.
DR InterPro; IPR000537; UbiA_prenyltransferase.
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 membrane; Magnesium; Membrane; Menaquinone biosynthesis;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..292
FT /note="1,4-dihydroxy-2-naphthoate octaprenyltransferase"
FT /id="PRO_0000096418"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
SQ SEQUENCE 292 AA; 30014 MW; FF73431AB309D817 CRC64;
MASFAQWVSG ARPRTLPNAI APVVAGTGAA AWLHAAVWWK ALLALAVAVA LVIGVNYAND
YSDGIRGTDD DRVGPVRLVG SRLATPRSVL TAAMTSLALG ALAGLVLALL SAPWLIAVGA
ICIAGAWLYT GGSKPYGYAG FGELAVFVFF GPVAVLGTQY TQALRVDWVG LAQAVATGAL
SCSVLVANNL RDIPTDARAD KITLAVRLGD ARTRMLYQGL LAVAGVLTFV LMLATPWCVV
GLVAAPLALR AAGPVRSGRG GRELIPVLRD TGLAMLVWAL AVAGALAFGQ LS
