ID D3SU22_NATMM Unreviewed; 300 AA.
AC D3SU22;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase {ECO:0000256|HAMAP-Rule:MF_01934};
DE Short=DHNA-CoA synthase {ECO:0000256|HAMAP-Rule:MF_01934};
DE EC=4.1.3.36 {ECO:0000256|HAMAP-Rule:MF_01934};
GN Name=menB {ECO:0000256|HAMAP-Rule:MF_01934,
GN ECO:0000313|EMBL:ADD07111.1};
GN OrderedLocusNames=Nmag_3561 {ECO:0000313|EMBL:ADD07111.1};
GN ORFNames=C500_12410 {ECO:0000313|EMBL:ELY28746.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD07111.1, ECO:0000313|Proteomes:UP000001879};
RN [1] {ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000001879};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA Maupin-Furlow J.A., Woyke T.;
RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD07111.1, ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD07111.1}, and ATCC 43099 / DSM
RC 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT "A comparative genomics perspective on the genetic content of the
RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL BMC Genomics 13:165-165(2012).
RN [3] {ECO:0000313|EMBL:ELY28746.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC {ECO:0000313|EMBL:ELY28746.1};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:ADD07111.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD07111.1};
RA Pfeiffer F.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-
CC naphthoyl-CoA (DHNA-CoA). {ECO:0000256|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:0000256|ARBA:ARBA00000177, ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_01934}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01934}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01934}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01934}.
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DR EMBL; CP001932; ADD07111.1; -; Genomic_DNA.
DR EMBL; AOHS01000040; ELY28746.1; -; Genomic_DNA.
DR RefSeq; WP_004267699.1; NZ_AOHS01000040.1.
DR AlphaFoldDB; D3SU22; -.
DR STRING; 547559.Nmag_3561; -.
DR PaxDb; 547559-Nmag_3561; -.
DR GeneID; 8826429; -.
DR KEGG; nmg:Nmag_3561; -.
DR PATRIC; fig|547559.17.peg.2453; -.
DR eggNOG; arCOG00240; Archaea.
DR HOGENOM; CLU_009834_7_7_2; -.
DR OrthoDB; 51339at2157; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000001879; Chromosome.
DR Proteomes; UP000011543; Unassembled WGS sequence.
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 CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 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 NCBIfam; TIGR01929; menB; 1.
DR PANTHER; PTHR43113:SF1; 1,4-DIHYDROXY-2-NAPHTHOYL-COA SYNTHASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43113; NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01934, ECO:0000313|EMBL:ADD07111.1};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01934};
KW Reference proteome {ECO:0000313|Proteomes:UP000001879}.
FT BINDING 43
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 88..92
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 100
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 143..147
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 170
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 176
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 273
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 100
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 171
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 273
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
SQ SEQUENCE 300 AA; 33431 MW; D5F4A372F5C06A6F CRC64;
MVSECFDADR WEPVDEFDFR DLTYHRAVDS GTVRIAFDRP DVRNAFRPGT VDELYDALDH
AKRQTDVGCI LLTGNGPSSK DGGWAFCSGG DQTVRGDDGY QYTGEDEESE TARASEQGRL
HILEVQRLIR HIPKVVVCVV PGWAVGGGHS LHVVCDMTLA SEEHAKFLQT DPDVASYDAG
FGSAYLAKQI GQKKAREVFF LGKTYSAEEA AEMGMVNEAV PHDELEETAL EWGERINAKS
PTAMRMLKYA FNMTDDGMIG QQVFAGEATR LGYMTDEAKE GRDAFVEGRD PEFDDYPWHY
//
