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Database: UniProt
Entry: B8I6K9_CLOCE
LinkDB: B8I6K9_CLOCE
Original site: B8I6K9_CLOCE 
ID   B8I6K9_CLOCE            Unreviewed;       284 AA.
AC   B8I6K9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE            Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102};
GN   Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
GN   OrderedLocusNames=Ccel_0519 {ECO:0000313|EMBL:ACL74901.1};
OS   Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Hungateiclostridiaceae; Ruminiclostridium.
OX   NCBI_TaxID=394503 {ECO:0000313|EMBL:ACL74901.1, ECO:0000313|Proteomes:UP000001349};
RN   [1] {ECO:0000313|EMBL:ACL74901.1, ECO:0000313|Proteomes:UP000001349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10
RC   {ECO:0000313|Proteomes:UP000001349};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E.,
RA   Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) 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}.
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};
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};
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}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102}.
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}.
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DR   EMBL; CP001348; ACL74901.1; -; Genomic_DNA.
DR   RefSeq; WP_015924074.1; NC_011898.1.
DR   STRING; 394503.Ccel_0519; -.
DR   EnsemblBacteria; ACL74901; ACL74901; Ccel_0519.
DR   KEGG; cce:Ccel_0519; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   HOGENOM; HOG000227155; -.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   OrthoDB; 803114at2; -.
DR   BioCyc; CCEL394503:G1GUL-522-MONOMER; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000001349; Chromosome.
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; 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.
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:UP000001349};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102};
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:UP000001349}.
FT   DOMAIN        1    128       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      132    254       DapB_C. {ECO:0000259|Pfam:PF05173}.
FT   NP_BIND     100    102       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   REGION      168    169       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    158    158       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    162    162       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   BINDING     159    159       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
SQ   SEQUENCE   284 AA;  31305 MW;  2CE565C0E117C8E3 CRC64;
     MKVCISGLGR TGKEIAKAIL LQNEIQLVSA ICSPTSKSLN KDLGEILGIN KTGITVTGSD
     KLEEVIFRNK PDVVIDFSNP KSALKNALIF SKYRINIVVG TTGFSDYQLK KLYVICRKFK
     NGIVYAPNIT MGVNVLMLLS NLTASLLSSY DFQITELHHK NKLDSPSGTA KKIAGEIQNG
     LSNKGVVVSH KDIPINSVRA GGVIGKHEVM IVGQEDKIEI SHESFSRKAF AQGAISAAKY
     IHKKSGYYEM KDVLDLEKVL QTYIENNNRS SRRRRKYDAK PASN
//
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