ID A0A177H4A2_9RHOB Unreviewed; 302 AA.
AC A0A177H4A2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:OAH05796.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:OAH05796.1};
GN Name=dapA_4 {ECO:0000313|EMBL:OAH05796.1};
GN ORFNames=pfor_37c3557 {ECO:0000313|EMBL:OAH05796.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH05796.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH05796.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH05796.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {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:OAH05796.1}.
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DR EMBL; LGRT01000038; OAH05796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H4A2; -.
DR STRING; 1689867.pfor_37c3557; -.
DR PATRIC; fig|1689867.3.peg.3605; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000077333; Unassembled WGS sequence.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128:SF73; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000077333}.
FT ACT_SITE 134
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 162
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 46
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 203
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 302 AA; 32873 MW; 7463AEB1E676ACA2 CRC64;
MQFEGIYTPL VTPYHDDFSL NEAALVETVE YLIAAGVHGI VVAGSTGEYY AQTPEERLEM
MTRCAGLING RVPMVTGTGA IRTEDSIMYA KAAKAAGADA LLVATPPYAY PTGREIALHA
LAVDRAANLP VMLYNYPGRM SVDMDEECLD RLGRSPNFCG IKESSGDINR LHMLARDYPH
IALSCGMDDQ ALEFFAWGAR SWVCAGSNFA PEAHIGLYEA CVIEGDFKKG RAIMSAMLPL
MRVLEQGGKF VQCIKYGLTL RGIDAGPPRK PLQPLNKDDK RELAEVIRTM NTAISSIKGA
NT
//
