位置:首页 > 蛋白库 > MENB_MYCTO
MENB_MYCTO
ID   MENB_MYCTO              Reviewed;         314 AA.
AC   P9WNP4; L0T442; O06414; Q7D9N7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01934};
DE            Short=DHNA-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01934};
DE            EC=4.1.3.36 {ECO:0000255|HAMAP-Rule:MF_01934};
GN   Name=menB {ECO:0000255|HAMAP-Rule:MF_01934}; OrderedLocusNames=MT0573;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-
CC       naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA +
CC         H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01934};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7.
CC       {ECO:0000255|HAMAP-Rule:MF_01934}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01934}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01934}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK44795.1; -; Genomic_DNA.
DR   PIR; G70547; G70547.
DR   AlphaFoldDB; P9WNP4; -.
DR   SMR; P9WNP4; -.
DR   EnsemblBacteria; AAK44795; AAK44795; MT0573.
DR   KEGG; mtc:MT0573; -.
DR   PATRIC; fig|83331.31.peg.604; -.
DR   HOGENOM; CLU_009834_7_7_11; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00167.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.12.10; -; 1.
DR   HAMAP; MF_01934; MenB; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR010198; DHNA-CoA_synthase_MenB.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   PANTHER; PTHR43113; PTHR43113; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR01929; menB; 1.
PE   3: Inferred from homology;
KW   Lyase; Menaquinone biosynthesis.
FT   CHAIN           1..314
FT                   /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT                   /id="PRO_0000427091"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         103..107
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         157..161
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   SITE            115
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   SITE            185
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   SITE            287
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
SQ   SEQUENCE   314 AA;  34689 MW;  AF2D192A9F607DC7 CRC64;
     MVAPAGEQGR SSTALSDNPF DAKAWRLVDG FDDLTDITYH RHVDDATVRV AFNRPEVRNA
     FRPHTVDELY RVLDHARMSP DVGVVLLTGN GPSPKDGGWA FCSGGDQRIR GRSGYQYASG
     DTADTVDVAR AGRLHILEVQ RLIRFMPKVV ICLVNGWAAG GGHSLHVVCD LTLASREYAR
     FKQTDADVGS FDGGYGSAYL ARQVGQKFAR EIFFLGRTYT AEQMHQMGAV NAVAEHAELE
     TVGLQWAAEI NAKSPQAQRM LKFAFNLLDD GLVGQQLFAG EATRLAYMTD EAVEGRDAFL
     QKRPPDWSPF PRYF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024