GenomeNet

Database: UniProt
Entry: A0A1M6SCR7_9FIRM
LinkDB: A0A1M6SCR7_9FIRM
Original site: A0A1M6SCR7_9FIRM 
ID   A0A1M6SCR7_9FIRM        Unreviewed;       252 AA.
AC   A0A1M6SCR7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081423};
DE            Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081445};
GN   Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
GN   ORFNames=SAMN02745243_02916 {ECO:0000313|EMBL:SHK42337.1};
OS   Hespellia stercorisuis DSM 15480.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Hespellia.
OX   NCBI_TaxID=1121950 {ECO:0000313|EMBL:SHK42337.1, ECO:0000313|Proteomes:UP000184301};
RN   [1] {ECO:0000313|EMBL:SHK42337.1, ECO:0000313|Proteomes:UP000184301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15480 {ECO:0000313|EMBL:SHK42337.1,
RC   ECO:0000313|Proteomes:UP000184301};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) =
CC         (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) =
CC         (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081412}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
CC       ECO:0000256|SAAS:SAAS01081435}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00102, ECO:0000256|SAAS:SAAS01081404}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate
CC       reductase (DHDPR), catalyzing the conversion of
CC       dihydrodipicolinate to tetrahydrodipicolinate. However, it was
CC       shown in E.coli that the substrate of the enzymatic reaction is
CC       not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-
CC       2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by
CC       the DapA-catalyzed reaction. {ECO:0000256|HAMAP-Rule:MF_00102}.
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; FQZY01000048; SHK42337.1; -; Genomic_DNA.
DR   RefSeq; WP_073111750.1; NZ_FQZY01000048.1.
DR   BioCyc; GCF_900142165:BUB85_RS14435-MONOMER; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000184301; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; 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-UniRule.
DR   HAMAP; MF_00102; DapB; 1.
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   PANTHER; PTHR20836; PTHR20836; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   PIRSF; PIRSF000161; DHPR; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00036; dapB; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081390};
KW   Complete proteome {ECO:0000313|Proteomes:UP000184301};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081408};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081418};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081406};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081420};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00333002};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS00333034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184301}.
FT   DOMAIN        2    112       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      115    250       DapB_C. {ECO:0000259|Pfam:PF05173}.
FT   NP_BIND       8     13       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND      85     87       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND     109    112       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   REGION      153    154       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    143    143       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    147    147       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   BINDING      34     34       NAD. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   BINDING     144    144       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
SQ   SEQUENCE   252 AA;  27477 MW;  4C5DE804354139E3 CRC64;
     MVKLIMHGCN GKMGRVITDI VKNDEHTELV AGVDSYTGVP NEYPVFESIE KCDVKADAII
     DFSNAAAVDG LLDYCVEKQV PVVLCTTGLS EEQLKKVEET AKKVAVLKSA NMSLGINMLL
     KLLQNATKVL APAGFDIEIV EKHHNQKVDA PSGTAIALAD SINETLDHEY KYVYDRSQVR
     EKRTKKEIGM SAVRGGSIVG EHEVIFAGAD EVIEFKHTAY SKAIFGKGAV EAAKFLADRQ
     AGLYDMSDVI QL
//
DBGET integrated database retrieval system