MENA_SYNY3
ID MENA_SYNY3 Reviewed; 307 AA.
AC P73962;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=2-carboxy-1,4-naphthoquinone phytyltransferase {ECO:0000255|HAMAP-Rule:MF_01938};
DE EC=2.5.1.130 {ECO:0000255|HAMAP-Rule:MF_01938, ECO:0000305|PubMed:10722690};
DE AltName: Full=1,4-dihydroxy-2-naphthoate phytyltransferase {ECO:0000255|HAMAP-Rule:MF_01938, ECO:0000303|PubMed:10722690};
DE Short=DHNA phytyltransferase {ECO:0000255|HAMAP-Rule:MF_01938, ECO:0000303|PubMed:10722690};
GN Name=menA {ECO:0000255|HAMAP-Rule:MF_01938}; OrderedLocusNames=slr1518;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=10722690; DOI=10.1074/jbc.275.12.8523;
RA Johnson T.W., Shen G., Zybailov B., Kolling D., Reategui R.,
RA Beauparlant S., Vassiliev I.R., Bryant D.A., Jones A.D., Golbeck J.H.,
RA Chitnis P.R.;
RT "Recruitment of a foreign quinone into the A(1) site of photosystem I. I.
RT Genetic and physiological characterization of phylloquinone biosynthetic
RT pathway mutants in Synechocystis sp. pcc 6803.";
RL J. Biol. Chem. 275:8523-8530(2000).
CC -!- FUNCTION: Involved in the synthesis of phylloquinone (vitamin K1).
CC Catalyzes the transfer of a prenyl chain to 2-carboxy-1,4-
CC naphthoquinone. {ECO:0000255|HAMAP-Rule:MF_01938,
CC ECO:0000305|PubMed:10722690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-dioxo-2-naphthoate + H(+) + phytyl diphosphate = CO2 +
CC demethylphylloquinone + diphosphate; Xref=Rhea:RHEA:47740,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:31087,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:75434, ChEBI:CHEBI:87842;
CC EC=2.5.1.130; Evidence={ECO:0000255|HAMAP-Rule:MF_01938,
CC ECO:0000305|PubMed:10722690};
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01938, ECO:0000269|PubMed:10722690}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01938, ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01938, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants grow photoautotrophically under low light
CC conditions, with doubling times twice that of the wild type, but they
CC are unable to grow under high light conditions. Mutants contain less
CC photosystem I (PSI) than the wild-type cells, and membranes do not
CC contain detectable levels of phylloquinone.
CC {ECO:0000269|PubMed:10722690}.
CC -!- SIMILARITY: Belongs to the MenA family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01938, ECO:0000305}.
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DR EMBL; BA000022; BAA18030.1; -; Genomic_DNA.
DR PIR; S75469; S75469.
DR AlphaFoldDB; P73962; -.
DR IntAct; P73962; 4.
DR STRING; 1148.1653114; -.
DR PaxDb; P73962; -.
DR EnsemblBacteria; BAA18030; BAA18030; BAA18030.
DR KEGG; syn:slr1518; -.
DR eggNOG; COG1575; Bacteria.
DR InParanoid; P73962; -.
DR OMA; QWIEGAR; -.
DR PhylomeDB; P73962; -.
DR BioCyc; MetaCyc:MON-13822; -.
DR UniPathway; UPA00995; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; 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:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
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_01938; MenA_2; 1.
DR InterPro; IPR011937; DHNA_phytyltransferase_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.
DR TIGRFAMs; TIGR02235; menA_cyano-plnt; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..307
FT /note="2-carboxy-1,4-naphthoquinone phytyltransferase"
FT /id="PRO_0000096419"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01938"
SQ SEQUENCE 307 AA; 33247 MW; 7107F9976D4F1C73 CRC64;
MTESSPLAPS TAPATRKLWL AAIKPPMYTV AVVPITVGSA VAYGLTGQWH GDVFTIFLLS
AIAIIAWINL SNDVFDSDTG IDVRKAHSVV NLTGNRNLVF LISNFFLLAG VLGLMSMSWR
AQDWTVLELI GVAIFLGYTY QGPPFRLGYL GLGELICLIT FGPLAIAAAY YSQSQSFSWN
LLTPSVFVGI STAIILFCSH FHQVEDDLAA GKKSPIVRLG TKLGSQVLTL SVVSLYLITA
IGVLCHQAPW QTLLIIASLP WAVQLIRHVG QYHDQPEQVS NCKFIAVNLH FFSGMLMAAG
YGWAGLG
