ID D5U450_BRAM5 Unreviewed; 298 AA.
AC D5U450;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ADG72231.1};
GN OrderedLocusNames=Bmur_2156 {ECO:0000313|EMBL:ADG72231.1};
OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS murdochii).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG72231.1, ECO:0000313|Proteomes:UP000001915};
RN [1] {ECO:0000313|EMBL:ADG72231.1, ECO:0000313|Proteomes:UP000001915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC {ECO:0000313|Proteomes:UP000001915};
RX PubMed=21304710; DOI=10.4056/sigs.831993;
RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL Stand. Genomic Sci. 2:260-269(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP001959; ADG72231.1; -; Genomic_DNA.
DR RefSeq; WP_013114602.1; NC_014150.1.
DR AlphaFoldDB; D5U450; -.
DR STRING; 526224.Bmur_2156; -.
DR KEGG; brm:Bmur_2156; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_6_0_12; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000001915; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 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; PS00665; DHDPS_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365}.
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 48
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 206
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 298 AA; 33517 MW; 5D3DF27DEB45D017 CRC64;
MNRCEGILSA LMTPFTKEGK LDENVLRKYV RHNIDHMKVD GLYVGGSTGE GLLMSKEERM
AVFEITKEEV AGKIPLIAHV GTLNLNEACE MANKAEELGY DLISAVTPYY YPFSFADISK
YYNTILNSTS KTPIVIYFLP TLSNNSISLD DFGKLFENDR VMGIKYTSSD LFLLERLKQK
FPTKMMWAGF DELLIAYASY GLRSGIGSTY NIQAPLAKKV IEAVEKKDME EALKIQHDMN
DVISTLLKVG IYPALKECIT FYDPSAVSYC RAPMGSKPLG DSEKSLLKDM FEKYLSKL
//
