ID Q8TVI0_METKA Unreviewed; 270 AA.
AC Q8TVI0;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase {ECO:0000256|HAMAP-Rule:MF_00960};
DE Short=ADH synthase {ECO:0000256|HAMAP-Rule:MF_00960};
DE Short=ADHS {ECO:0000256|HAMAP-Rule:MF_00960};
DE Short=ADTH synthase {ECO:0000256|HAMAP-Rule:MF_00960};
DE EC=2.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00960};
GN Name=fbaB {ECO:0000313|EMBL:AAM02622.1};
GN Synonyms=aroA' {ECO:0000256|HAMAP-Rule:MF_00960};
GN OrderedLocusNames=MK1409 {ECO:0000313|EMBL:AAM02622.1};
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC Methanopyraceae; Methanopyrus.
OX NCBI_TaxID=190192 {ECO:0000313|EMBL:AAM02622.1, ECO:0000313|Proteomes:UP000001826};
RN [1] {ECO:0000313|EMBL:AAM02622.1, ECO:0000313|Proteomes:UP000001826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938
RC {ECO:0000313|Proteomes:UP000001826};
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC -!- FUNCTION: Catalyzes a transaldol reaction between 6-deoxy-5-
CC ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with
CC an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-
CC dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an
CC alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ),
CC which is involved in the canonical pathway for the biosynthesis of
CC aromatic amino acids. {ECO:0000256|HAMAP-Rule:MF_00960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-
CC semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-
CC lyxo-hept-6-ulosonate; Xref=Rhea:RHEA:25952, ChEBI:CHEBI:58859,
CC ChEBI:CHEBI:58860, ChEBI:CHEBI:58861, ChEBI:CHEBI:537519;
CC EC=2.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00960};
CC -!- SUBUNIT: Homodecamer. {ECO:0000256|HAMAP-Rule:MF_00960}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00960}.
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DR EMBL; AE009439; AAM02622.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TVI0; -.
DR STRING; 190192.MK1409; -.
DR PaxDb; 190192-MK1409; -.
DR EnsemblBacteria; AAM02622; AAM02622; MK1409.
DR KEGG; mka:MK1409; -.
DR PATRIC; fig|190192.8.peg.1564; -.
DR HOGENOM; CLU_057069_2_0_2; -.
DR InParanoid; Q8TVI0; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0016744; F:transketolase or transaldolase activity; 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 CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00960; ADH_synthase; 1.
DR InterPro; IPR010210; ADH_synthase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR NCBIfam; TIGR01949; ADH_synth; 1.
DR PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00960};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00960};
KW Reference proteome {ECO:0000313|Proteomes:UP000001826};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00960};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00960}.
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960,
FT ECO:0000256|PIRSR:PIRSR038992-1"
FT ACT_SITE 178
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000256|PIRSR:PIRSR038992-1"
FT ACT_SITE 178
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT BINDING 27..31
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT BINDING 147..149
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT BINDING 203..204
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
FT BINDING 231..232
FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58861"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960"
SQ SEQUENCE 270 AA; 29118 MW; B74F66C5CE2FCCD6 CRC64;
MVHIGKQIRM ERIMNRETGR TLIVPMDHGV TLGPITGLED LEETVDAVAR GGANAVLLHK
GMVRAGHRGY GRDVGLIIHL SASTELGPDP NNKVLVSRVE EAIRLGADAV SVHVNVGAED
EPQMLKKLGE IAARCSDWGM PLVAMMYPRG PKVEDEFDVE YVKHAARVGA ELGADIVKTN
YTGDPDSFRE VVKGCPVPVV IAGGPKAETP KEVLEMVKGA IEAGAAGAAI GRNIFAHKSP
RMREAMTRAI ARIIHEDAEV EEAMKELERV
//
