(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9C2_METMS

ID   D5E9C2_METMS            Unreviewed;       380 AA.
AC   D5E9C2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 46.
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:0000256|HAMAP-Rule:MF_01244};
GN   OrderedLocusNames=Mmah_0240 {ECO:0000313|EMBL:ADE35773.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35773.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35773.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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; CP001994; ADE35773.1; -; Genomic_DNA.
DR   RefSeq; WP_013036716.1; NC_014002.1.
DR   EnsemblBacteria; ADE35773; ADE35773; Mmah_0240.
DR   GeneID; 8982372; -.
DR   KEGG; mmh:Mmah_0240; -.
DR   eggNOG; arCOG04353; Archaea.
DR   eggNOG; COG1465; LUCA.
DR   HOGENOM; HOG000015603; -.
DR   KO; K11646; -.
DR   OMA; GDRVCID; -.
DR   OrthoDB; 29853at2157; -.
DR   BioCyc; MMAH547558:G1GHT-238-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
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: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; PTHR33563; 1.
DR   Pfam; PF01959; DHQS; 1.
DR   PIRSF; PIRSF006655; DHQ_synth; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9C2.
DR   SWISS-2DPAGE; D5E9C2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01244};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01244};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01244};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
SQ   SEQUENCE   380 AA;  41434 MW;  58D0EE162DEB0650 CRC64;
     MKKQVWIRAD EGDWEDKKER ITGGLESGAD CVLVEAEDVD KTKELGDIKI AAFTDNADTA
     ADIIVIGRGG EGDGTLPLPV DMSNSRDFEQ LATLRRQKKS IAALVVIQDK KYEKFAAAIG
     TECDYLIAIG TDWKVIPLEN LIAQLQEKEV NIISGVRDAD EAKLALETME HGSDGVLLDT
     ANPDTLKKTV KLAEEAGVEG IDLVPATITR IEPVGMGDRV CVDTCNLMER GEGMLVGSQS
     AGMFLVHSES EESPYVASRP FRVNAGAVHA YVKVGDKTRY LSELEAGDEV TIVNTEGQQR
     KGIVGRVKIE RRPLMLVEAQ SKDGKTVKNI LQNAETIKLV STSKEPVSIA SLKEGDEVLV
     HMEDTGRHFG MKVQETIIEK
//

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