(data stored in SCRATCH zone)

SWISSPROT: A0KFP0_AERHH

ID   A0KFP0_AERHH            Unreviewed;       307 AA.
AC   A0KFP0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   13-FEB-2019, entry version 75.
DE   RecName: Full=1,4-dihydroxy-2-naphthoate octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01937};
DE            Short=DHNA-octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01937};
DE            EC=2.5.1.74 {ECO:0000256|HAMAP-Rule:MF_01937};
GN   Name=menA {ECO:0000256|HAMAP-Rule:MF_01937,
GN   ECO:0000313|EMBL:ABK39485.1};
GN   OrderedLocusNames=AHA_0533 {ECO:0000313|EMBL:ABK39485.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39485.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39485.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC       demethylmenaquinone (DMK). {ECO:0000256|HAMAP-Rule:MF_01937}.
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;
CC         EC=2.5.1.74; Evidence={ECO:0000256|HAMAP-Rule:MF_01937};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC       menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01937}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01937}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01937}.
CC   -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01937}.
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DR   EMBL; CP000462; ABK39485.1; -; Genomic_DNA.
DR   RefSeq; WP_011704506.1; NC_008570.1.
DR   RefSeq; YP_855066.1; NC_008570.1.
DR   STRING; 380703.AHA_0533; -.
DR   EnsemblBacteria; ABK39485; ABK39485; AHA_0533.
DR   GeneID; 4488873; -.
DR   KEGG; aha:AHA_0533; -.
DR   PATRIC; fig|380703.7.peg.526; -.
DR   eggNOG; ENOG4105EIS; Bacteria.
DR   eggNOG; COG1575; LUCA.
DR   HOGENOM; HOG000028297; -.
DR   KO; K02548; -.
DR   OMA; PPMYSVA; -.
DR   BioCyc; AHYD380703:G1G7B-534-MONOMER; -.
DR   UniPathway; UPA00079; UER00168.
DR   Proteomes; UP000000756; 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:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01937; MenA_1; 1.
DR   InterPro; IPR004657; MenA.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR026046; UBIAD1.
DR   Pfam; PF01040; UbiA; 1.
DR   PIRSF; PIRSF005355; UBIAD1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFP0.
DR   SWISS-2DPAGE; A0KFP0.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01937};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01937};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01937};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01937};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01937,
KW   ECO:0000313|EMBL:ABK39485.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01937};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01937}.
FT   TRANSMEM     98    117       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01937}.
FT   TRANSMEM    123    147       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01937}.
FT   TRANSMEM    159    177       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01937}.
FT   TRANSMEM    183    202       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01937}.
FT   TRANSMEM    229    248       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01937}.
FT   TRANSMEM    289    306       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01937}.
SQ   SEQUENCE   307 AA;  32512 MW;  9E9115CBA5EA5124 CRC64;
     MFGHHNMTNT LSIWLLAARL RTLPLACSSI LLGSGLAASR GAFDGTIMAL SLLTAILLQI
     LSNLANDYGD AVSGADNGER IGPQRAVVSG LITRRQMCVA MALTALAAVV SGLALLGCAF
     GDQWLQILTF VLLGGAAIVA AITYTVGKTP YGYRGFGDIS VFLFFGLLGV LGSYYLFTKT
     LQWDLLLPAT ACGLLATAVL NINNVRDIET DAVSGKITLA VRLGRNRAIA YHWVLLGAAL
     LTTIAFLLTQ PASFWPWIFL PAMKPLTDAA KTLRQSFDGE VLTGALKKTA ISAFLFSLLL
     SIGLALS
//

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