ID A0A1W9PBX4_9BACT Unreviewed; 183 AA.
AC A0A1W9PBX4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000313|EMBL:OQX55722.1};
DE Flags: Fragment;
GN ORFNames=B5M53_03935 {ECO:0000313|EMBL:OQX55722.1};
OS Candidatus Cloacimonas sp. 4484_209.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1968525 {ECO:0000313|EMBL:OQX55722.1, ECO:0000313|Proteomes:UP000192614};
RN [1] {ECO:0000313|Proteomes:UP000192614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapB family.
CC {ECO:0000256|ARBA:ARBA00006642}.
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:OQX55722.1}.
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DR EMBL; MZGI01000057; OQX55722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9PBX4; -.
DR Proteomes; UP000192614; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR InterPro; IPR022663; DapB_C.
DR InterPro; IPR000846; DapB_N.
DR InterPro; IPR022664; DapB_N_CS.
DR InterPro; IPR023940; DHDPR_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00036; dapB; 1.
DR PANTHER; PTHR20836:SF7; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE; 1.
DR PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1.
DR Pfam; PF05173; DapB_C; 1.
DR Pfam; PF01113; DapB_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01298; DAPB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 2..44
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 47..180
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQX55722.1"
SQ SEQUENCE 183 AA; 20339 MW; CCC456461026D424 CRC64;
VNMVKFAVQH LKPIIIGTTA LGDEDNKKIL EASHKIAVLK ASNMSVGTNV IFAMLKKLPD
ILYKNFDIEI SEIHHSKKKD SPSGTARTMG KIISERKENA HFRYGREGNE LKRESGEIGF
HSIRGGTVAG IHTVYFLGDD ESIEITHRVY SKRIFAIGAI AAAKWIFKKK PGIYSMQDLI
VSG
//