ID A0A2M9PBR4_9RHOB Unreviewed; 330 AA.
AC A0A2M9PBR4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086, ECO:0000256|HAMAP-Rule:MF_00418};
DE Short=HTPA synthase {ECO:0000256|HAMAP-Rule:MF_00418};
DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086, ECO:0000256|HAMAP-Rule:MF_00418};
GN Name=dapA {ECO:0000256|HAMAP-Rule:MF_00418};
GN ORFNames=CNY89_11195 {ECO:0000313|EMBL:PJN94980.1};
OS Amaricoccus sp. HAR-UPW-R2A-40.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Amaricoccus.
OX NCBI_TaxID=1985299 {ECO:0000313|EMBL:PJN94980.1, ECO:0000313|Proteomes:UP000232137};
RN [1] {ECO:0000313|EMBL:PJN94980.1, ECO:0000313|Proteomes:UP000232137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAR-UPW-R2A-40 {ECO:0000313|EMBL:PJN94980.1,
RC ECO:0000313|Proteomes:UP000232137};
RA Kumari P., Krishnamurthi S.;
RT "HAR-UPW-R2A-40 Amaricoccus sp.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000256|ARBA:ARBA00003294, ECO:0000256|HAMAP-Rule:MF_00418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-
CC hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000594, ECO:0000256|HAMAP-
CC Rule:MF_00418};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00005120, ECO:0000256|HAMAP-Rule:MF_00418}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_00418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|HAMAP-
CC Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJN94980.1}.
CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase
CC (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was
CC shown in E.coli that the product of the enzymatic reaction is not
CC dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-
CC dipicolinic acid (HTPA), and that the consecutive dehydration reaction
CC leading to DHDP is not spontaneous but catalyzed by DapB.
CC {ECO:0000256|HAMAP-Rule:MF_00418}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PHNO01000664; PJN94980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9PBR4; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000232137; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd00950; DHDPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00418; DapA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005263; DapA.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR NCBIfam; TIGR00674; dapA; 1.
DR PANTHER; PTHR12128:SF66; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00418};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00418};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_00418};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_00418}; Reference proteome {ECO:0000313|Proteomes:UP000232137};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00418}.
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 199
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 83
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 241
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-2"
FT SITE 82
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT SITE 145
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ SEQUENCE 330 AA; 35743 MW; C9E42EDB20F28C28 CRC64;
MIRSGGPDPV RSSARGRQRG LQDGRVASNR ARHIAQESRH VQRFDHRARH PLRERKVDEK
ALVELVEWQI AEGTHGVVPV GTTGETPTLT HDEHEHVIEV VVATAAGRIP VIAGAGSNNT
DEAIRLMRFA KKVGADAALV VTPYYNKPNQ RGLIAHYTAL HDAVDLPIVI YNIPGRSVID
MTPATMGELA RLPRIVGVKD ATGDVTRVSD QRAACGADFI QLSGEDASAL GFNAHGGVGC
ISVVSNIAPR LCAEFQTATL NGDWTKALAL QDRLLPLHRA AFAEPNPGPT KYALSLLGKC
QEEMRLPLVP IEELTRERVR AALRHAGLLN
//