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Database: UniProt
Entry: D3SZV2_NATMM
LinkDB: D3SZV2_NATMM
Original site: D3SZV2_NATMM 
ID   D3SZV2_NATMM            Unreviewed;       429 AA.
AC   D3SZV2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE            Short=DHQ synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE            EC=1.4.1.24 {ECO:0000256|HAMAP-Rule:MF_01244};
DE   AltName: Full=3-dehydroquinate synthase II {ECO:0000256|HAMAP-Rule:MF_01244};
GN   Name=aroB {ECO:0000313|EMBL:ADD06362.1};
GN   Synonyms=aroB' {ECO:0000256|HAMAP-Rule:MF_01244};
GN   OrderedLocusNames=Nmag_2808 {ECO:0000313|EMBL:ADD06362.1};
GN   ORFNames=C500_06366 {ECO:0000313|EMBL:ELY31495.1};
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:ADD06362.1, 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:ADD06362.1, ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06362.1}, 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:ELY31495.1, 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:ELY31495.1};
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:ADD06362.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06362.1};
RA   Pfeiffer F.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative deamination and cyclization of 2-
CC       amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-
CC       dehydroquinate (DHQ), which is fed into the canonical shikimic pathway
CC       of aromatic amino acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)
CC         = 3-dehydroquinate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:25956,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58859; EC=1.4.1.24; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01244};
CC   -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01244}.
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DR   EMBL; CP001932; ADD06362.1; -; Genomic_DNA.
DR   EMBL; AOHS01000026; ELY31495.1; -; Genomic_DNA.
DR   RefSeq; WP_004214898.1; NZ_AOHS01000026.1.
DR   AlphaFoldDB; D3SZV2; -.
DR   STRING; 547559.Nmag_2808; -.
DR   PaxDb; 547559-Nmag_2808; -.
DR   GeneID; 8825664; -.
DR   KEGG; nmg:Nmag_2808; -.
DR   PATRIC; fig|547559.17.peg.1233; -.
DR   eggNOG; arCOG04353; Archaea.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OrthoDB; 10265at2157; -.
DR   Proteomes; UP000001879; Chromosome.
DR   Proteomes; UP000011543; Unassembled WGS sequence.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0102042; F:dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR   InterPro; IPR002812; DHQ_synth.
DR   PANTHER; PTHR33563; -; 1.
DR   PANTHER; PTHR33563:SF1; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   Pfam; PF01959; DHQS; 1.
DR   PIRSF; PIRSF006655; DHQ_synth; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01244};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_01244}; Lyase {ECO:0000313|EMBL:ELY31495.1};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01244};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01244}; Reference proteome {ECO:0000313|Proteomes:UP000001879}.
SQ   SEQUENCE   429 AA;  46555 MW;  34F7A2435930AEF2 CRC64;
     MTRSVWIKAD DTVGDWDDRR ARITAALEAG ADWVLVDEKD VERVRELGDI NVAAFRTDGD
     VTLVDDAEAD VDDDTDTEST GVDELDEIDN VGDPENLDVE LSAETGNGTA ADAVIVGKDG
     EGDATIDLPN DFSGSADLST LRRDGDKDID RGAYVRILDT EYEAFAEAAA EEGEYTIVIG
     EDWTIIPLEN LIARIGEETD LIAGVTSAEE AKTAFETLEL GSDAVLLDSD NPDEIRRTVE
     VRDEAERESL DLQYAEVTDV EQIGSADRVC VDTGSLLEHD EGMLVGSMSR GLVFVHAETA
     ESPYVASRPF RVNAGAVHAY VRTPDGGTKY LSELQSGDEV QVVDTNGNTR EAIVGRVKIE
     KRPMFRVALE TDDGDHIETL LQNAETIKVA TGDGRTAVTD LAAGDELLLY YEDTARHFGE
     AVEESIIEK
//
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