ID K9F0C9_9ACTO Unreviewed; 302 AA.
AC K9F0C9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dihydrodipicolinate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9233_01359 {ECO:0000313|EMBL:EKU94905.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU94905.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU94905.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL Submitted (SEP-2012) 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:EKU94905.1}.
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DR EMBL; AGWL01000007; EKU94905.1; -; Genomic_DNA.
DR RefSeq; WP_007001565.1; NZ_JH992955.1.
DR AlphaFoldDB; K9F0C9; -.
DR STRING; 202789.GCA_001457435_00750; -.
DR PATRIC; fig|883066.3.peg.1423; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_11; -.
DR Proteomes; UP000009888; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000009888};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 133
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 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 302 AA; 32738 MW; 355249680161266A CRC64;
MSAKFLSPSI TAFTESRDVD EKGCLSQWQR LIENGVDGLL ILGSMGEFFA LTSKQKRQLI
ELATSQLAGK THLMFGTGCN GVEETVELSN FAFQKGADSV ILIAPYYMAL SEDDLFAHFS
SVAHRVSGPI YLYNFPARTG NPITASLLVR LLAENENIVG IKDTIPDVAG TRALMAAIKE
ERPGFEFFSG MDENFFHNAL SEGAGCIAGL SNVFPELTSA AVRAFANADF GGMSEIQRAI
NEASGLYNIV SFFPMAIKEA TRLRGVAIEP YSAATPTVLS SREREQVVAV VQRVETLLNS
IN
//
