(data stored in ACNUC7421 zone)

SWISSPROT: A0KFN6_AERHH

ID   A0KFN6_AERHH            Unreviewed;       286 AA.
AC   A0KFN6;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 84.
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:ABK38664.1};
GN   OrderedLocusNames=AHA_0529 {ECO:0000313|EMBL:ABK38664.1};
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:ABK38664.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38664.1, 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: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-
CC       dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000256|HAMAP-
CC       Rule:MF_01934}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-
CC         CoA + H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57364, ChEBI:CHEBI:58897;
CC         EC=4.1.3.36; Evidence={ECO:0000256|HAMAP-Rule:MF_01934};
CC   -!- COFACTOR:
CC       Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01934};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step
CC       6/7. {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.
CC       MenB subfamily. {ECO:0000256|HAMAP-Rule:MF_01934}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01934}.
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DR   EMBL; CP000462; ABK38664.1; -; Genomic_DNA.
DR   RefSeq; WP_011704502.1; NC_008570.1.
DR   RefSeq; YP_855062.1; NC_008570.1.
DR   STRING; 380703.AHA_0529; -.
DR   EnsemblBacteria; ABK38664; ABK38664; AHA_0529.
DR   GeneID; 4488869; -.
DR   KEGG; aha:AHA_0529; -.
DR   PATRIC; fig|380703.7.peg.522; -.
DR   eggNOG; ENOG4108IPT; Bacteria.
DR   eggNOG; COG0447; LUCA.
DR   HOGENOM; HOG000027942; -.
DR   KO; K01661; -.
DR   OMA; IFKQTDA; -.
DR   BioCyc; AHYD380703:G1G7B-530-MONOMER; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00167.
DR   Proteomes; UP000000756; 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;
DR   PRODOM; A0KFN6.
DR   SWISS-2DPAGE; A0KFN6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01934, ECO:0000313|EMBL:ABK38664.1};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01934};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   REGION       85     89       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01934}.
FT   REGION      130    134       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01934}.
FT   REGION      155    157       Hydrogencarbonate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01934}.
FT   BINDING      46     46       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01934}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01934}.
FT   BINDING     156    156       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01934}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01934}.
FT   BINDING     259    259       Substrate; shared with neighboring
FT                                subunit. {ECO:0000256|HAMAP-Rule:
FT                                MF_01934}.
FT   BINDING     274    274       Substrate; shared with neighboring
FT                                subunit. {ECO:0000256|HAMAP-Rule:
FT                                MF_01934}.
FT   SITE         98     98       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01934}.
FT   SITE        259    259       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01934}.
SQ   SEQUENCE   286 AA;  31925 MW;  59EAE3897B55057C CRC64;
     MIEAMTEAEL YAPVEWRDCS AGYEDILYHK SDDGIAKITI NRPQVRNAFR PRTVKEMLQA
     LADARYDDQI GTIILTGFGE KAFCAGGDQK IRGDYGGYRD DEGTHHLNVL DFQRDIRTCP
     KPVVAMVAGY AVGGGHVLHM MCDLTIAADN AQFGQTGPKV GSFDGGWGAS YMARIVGQKK
     AREIWFLCRM YDAKQALDMG LVNTVVPLAE LERETVRWCR EMLQNSPMAL RCLKAALNAD
     CDGQAGLQEL AGNATMLFYM TEEGQEGRNA FNEKRRPDFS KYKRNP
//

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