ID T2G8N9_MEGG1 Unreviewed; 325 AA.
AC T2G8N9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 28-JAN-2026, entry version 43.
DE SubName: Full=Putative 3-dehydroquinate synthase {ECO:0000313|EMBL:AGW12501.1};
GN ORFNames=DGI_0593 {ECO:0000313|EMBL:AGW12501.1};
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448 {ECO:0000313|EMBL:AGW12501.1, ECO:0000313|Proteomes:UP000016587};
RN [1] {ECO:0000313|EMBL:AGW12501.1, ECO:0000313|Proteomes:UP000016587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000313|Proteomes:UP000016587};
RX PubMed=23974026; DOI=10.1128/JB.00411-13;
RA Morais-Silva F.O., Santos C.I., Rodrigues R., Pereira I.A.,
RA Rodrigues-Pousada C.;
RT "Roles of HynAB and Ech, the only two hydrogenases found in the model
RT sulfate reducer Desulfovibrio gigas.";
RL J. Bacteriol. 195:4753-4760(2013).
RN [2] {ECO:0000313|Proteomes:UP000016587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000313|Proteomes:UP000016587};
RA Morais-Silva F.O., Rezende A.M., Pimentel C., Resende D.M., Santos C.I.,
RA Clemente C., de Oliveira L.M., da Silva S.M., Costa D.A., Varela-Raposo A.,
RA Horacio E.C.A., Matos M., Flores O., Ruiz J.C., Rodrigues-Pousada C.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP006585; AGW12501.1; -; Genomic_DNA.
DR RefSeq; WP_021759154.1; NC_022444.1.
DR AlphaFoldDB; T2G8N9; -.
DR STRING; 1121448.DGI_0593; -.
DR KEGG; dgg:DGI_0593; -.
DR PATRIC; fig|1121448.10.peg.593; -.
DR eggNOG; COG1465; Bacteria.
DR HOGENOM; CLU_056379_0_0_7; -.
DR OrthoDB; 2043123at2; -.
DR Proteomes; UP000016587; Chromosome.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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-KW.
DR InterPro; IPR002812; DHQS.
DR InterPro; IPR030960; DHQS/DOIS_N.
DR InterPro; IPR056179; DHQS_C.
DR NCBIfam; NF002628; PRK02290.1-6; 1.
DR PANTHER; PTHR33563; -; 1.
DR PANTHER; PTHR33563:SF1; 3-DEHYDROQUINATE SYNTHASE; 1.
DR Pfam; PF01959; DHQS; 1.
DR Pfam; PF26558; DHQS_2nd; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Reference proteome {ECO:0000313|Proteomes:UP000016587}.
FT DOMAIN 1..134
FT /note="3-dehydroquinate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01959"
FT DOMAIN 149..324
FT /note="3-dehydroquinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF26558"
SQ SEQUENCE 325 AA; 34652 MW; D10D6F5FB352EF29 CRC64;
MKTVYFKALP YEKSLVTLAL ESGVDGVIVD PEHVEDVKAL SRVEALTPAD FTAICLTAKA
DEEQAVTCLM AGDKVILTKG WEIIPVENIL AQSTGLGVEV DNLDQARLAA GILERGVDFL
VVNPEAAPEL KTIVQEIKLS QGRIELATAT ITAIASAGLG HRVCVDTMSV FKSGQGMLVG
NSSAFTFLVN AETESNPYVA ARPFRINAGA VHAYALMPGD KTCYLEEVTS GREVLIVGHD
GATTVATVGR AKVEVRPMLR IDAEIKATGQ KGAIFLQNAE TIRLVHPGGQ PVSVVTLKVG
DDVLVNADAP GRHFGMRIQE QIKEH
//
