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MENB_STAHJ
ID   MENB_STAHJ              Reviewed;         272 AA.
AC   Q4L549;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=SH1917;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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   -!- COFACTOR:
CC       Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544;
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}.
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DR   EMBL; AP006716; BAE05226.1; -; Genomic_DNA.
DR   RefSeq; WP_011276187.1; NC_007168.1.
DR   AlphaFoldDB; Q4L549; -.
DR   SMR; Q4L549; -.
DR   STRING; 279808.SH1917; -.
DR   EnsemblBacteria; BAE05226; BAE05226; SH1917.
DR   GeneID; 58061967; -.
DR   KEGG; sha:SH1917; -.
DR   eggNOG; COG0447; Bacteria.
DR   HOGENOM; CLU_009834_7_7_9; -.
DR   OMA; IFKQTDA; -.
DR   OrthoDB; 1275789at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00167.
DR   Proteomes; UP000000543; 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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Menaquinone biosynthesis.
FT   CHAIN           1..272
FT                   /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT                   /id="PRO_0000224822"
FT   REGION          253..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33
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         72..76
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         84
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         116..120
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         141..143
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         142
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         148
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         245
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   SITE            84
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT   SITE            245
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
SQ   SEQUENCE   272 AA;  30383 MW;  A3F4CE6F61667B67 CRC64;
     MTRQWETLRE YDEIKYEFYE GIAKVTINRP EVRNAFTPKT VAEMIDAFSR ARDDQNISVI
     ILTGEGDKAF CSGGDQKKRG HGGYVGEDQI PRLNVLDLQR LIRVIPKPVI AMVRGYAIGG
     GNVLNVVCDL TIAADNAIFG QTGPKVGSFD AGYGSGYLAR IVGHKKAREI WYLCRQYNAQ
     EALDMGLVNT VVPLDQIEDE TVQWCKEIMK HSPTALRFLK AAMNADTDGL AGLQQMAGDA
     TLLYYTTDEA KEGRDAFKEK RDPDFDQFPK FP
 
 
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