GenomeNet

Database: UniProt
Entry: F4KKM8_PORAD
LinkDB: F4KKM8_PORAD
Original site: F4KKM8_PORAD 
ID   F4KKM8_PORAD            Unreviewed;       241 AA.
AC   F4KKM8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|SAAS:SAAS01081423};
DE            EC=1.17.1.8 {ECO:0000256|SAAS:SAAS01081445};
GN   OrderedLocusNames=Poras_1010 {ECO:0000313|EMBL:AEE12953.1};
OS   Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC
OS   10618 / JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides
OS   asaccharolyticus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12953.1, ECO:0000313|Proteomes:UP000006545};
RN   [1] {ECO:0000313|Proteomes:UP000006545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC   {ECO:0000313|Proteomes:UP000006545};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Pagani I., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {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;
CC         Evidence={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;
CC         Evidence={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|SAAS:SAAS01081412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01081435}.
CC   -!- SIMILARITY: Belongs to the DapB family.
CC       {ECO:0000256|SAAS:SAAS01081404}.
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; CP002689; AEE12953.1; -; Genomic_DNA.
DR   RefSeq; WP_013760424.1; NC_015501.1.
DR   STRING; 879243.Poras_1010; -.
DR   EnsemblBacteria; AEE12953; AEE12953; Poras_1010.
DR   KEGG; pah:Poras_1010; -.
DR   eggNOG; ENOG4105DUK; Bacteria.
DR   eggNOG; COG0289; LUCA.
DR   KO; K00215; -.
DR   OMA; RESFMPG; -.
DR   OrthoDB; 803114at2; -.
DR   BioCyc; PASA879243:G1GX8-1050-MONOMER; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000006545; 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:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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|SAAS:SAAS01081390};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006545};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01081408};
KW   Diaminopimelate biosynthesis {ECO:0000256|SAAS:SAAS01081418};
KW   Lysine biosynthesis {ECO:0000256|SAAS:SAAS01081406};
KW   NAD {ECO:0000256|SAAS:SAAS01081420};
KW   NADP {ECO:0000256|SAAS:SAAS00333002};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00333034,
KW   ECO:0000313|EMBL:AEE12953.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006545}.
FT   DOMAIN        1    104       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      107    237       DapB_C. {ECO:0000259|Pfam:PF05173}.
SQ   SEQUENCE   241 AA;  26352 MW;  EB8A9184D1F7EBB3 CRC64;
     MKIAILGYGR MGHMIEEVAT QRGHEVVARI DKTDAALLED GSLREADVAI EFSTPESGYQ
     LCQAALKAGL PVVTGSTGWK EQLEALKAEV QSSGRGGLFA ASNFSLGMNL MMILNEQLAQ
     LMAPYPEYTP RIQETHHIHK LDAPSGTAIT LAEGLIKQTP SLHDWHLGVE THDGSLGIEA
     IREGEVPGIH TVIYHSDIDE ITLRHEAYSR RGFALGATLA AEYLLQHPVG VWSMRDLILH
     K
//
DBGET integrated database retrieval system