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MENA_HAEIN
ID   MENA_HAEIN              Reviewed;         308 AA.
AC   P44739;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 117.
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};
GN   Name=menA {ECO:0000255|HAMAP-Rule:MF_01937}; OrderedLocusNames=HI_0509;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC       demethylmenaquinone (DMK). {ECO:0000255|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; EC=2.5.1.74;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01937};
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}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01937}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01937}.
CC   -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01937}.
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DR   EMBL; L42023; AAC22167.1; -; Genomic_DNA.
DR   PIR; H64153; H64153.
DR   RefSeq; NP_438667.2; NC_000907.1.
DR   AlphaFoldDB; P44739; -.
DR   SMR; P44739; -.
DR   STRING; 71421.HI_0509; -.
DR   EnsemblBacteria; AAC22167; AAC22167; HI_0509.
DR   KEGG; hin:HI_0509; -.
DR   PATRIC; fig|71421.8.peg.528; -.
DR   eggNOG; COG1575; Bacteria.
DR   HOGENOM; CLU_043611_1_1_6; -.
DR   OMA; QWIEGAR; -.
DR   PhylomeDB; P44739; -.
DR   UniPathway; UPA00079; UER00168.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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   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   3: Inferred from homology;
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_0000096415"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        47..67
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        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
SQ   SEQUENCE   308 AA;  33346 MW;  7A873AFC8071AF6B CRC64;
     MRSKKMINEK LKMWWETARP KTLPLALASI FTGSALGYWA NPQGFNGLVM VLCLLTTILL
     QVLSNFANDY GDHQKGSDTE ERIGPLRGIQ KGAISAKELK WGLILMVMAS FLSGSFLIGI
     AYENLSDLFA FAGLGILAIV AAITYTVGVK PYGYMGLGDI SVLVFFGLLG VGGTYYLQTH
     SIDSHIILPA IGSGLLASAV LNINNLRDIE QDAKAGKNTL AVRLGAYKGR VYHCILLSVA
     ALCYLAFAVA TAISWTNYLF VLAMPLLAKH AIFVYCSQQP SELRPILAQM SMISLLINIL
     FSLGLLIG
 
 
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