位置:首页 > 蛋白库 > DAPB_NEIG1
DAPB_NEIG1
ID   DAPB_NEIG1              Reviewed;         269 AA.
AC   Q5F5Y7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE            Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102};
GN   Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; OrderedLocusNames=NGO1781;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC       (HTPA) to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-
CC         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:0000255|HAMAP-
CC         Rule:MF_00102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-
CC         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:0000255|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:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00102}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate reductase
CC       (DHDPR), catalyzing the conversion of dihydrodipicolinate to
CC       tetrahydrodipicolinate. However, it was shown in E.coli that the
CC       substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP)
CC       but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
CC       (HTPA), the product released by the DapA-catalyzed reaction.
CC       {ECO:0000305}.
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; AE004969; AAW90400.1; -; Genomic_DNA.
DR   RefSeq; WP_003689993.1; NC_002946.2.
DR   RefSeq; YP_208812.1; NC_002946.2.
DR   PDB; 6BDX; X-ray; 1.85 A; A=1-269.
DR   PDBsum; 6BDX; -.
DR   AlphaFoldDB; Q5F5Y7; -.
DR   SMR; Q5F5Y7; -.
DR   STRING; 242231.NGO_1781; -.
DR   EnsemblBacteria; AAW90400; AAW90400; NGO_1781.
DR   GeneID; 66754361; -.
DR   KEGG; ngo:NGO_1781; -.
DR   PATRIC; fig|242231.10.peg.2138; -.
DR   HOGENOM; CLU_047479_2_1_4; -.
DR   OMA; HHPNKAD; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000000535; 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; 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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..269
FT                   /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT                   /id="PRO_0000228364"
FT   ACT_SITE        156
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         99..101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         123..126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         157
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         166..167
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   TURN            41..44
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   TURN            47..52
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           63..68
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           79..92
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          95..98
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           128..143
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          149..156
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           166..178
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          202..209
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          215..223
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          226..234
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           238..251
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:6BDX"
FT   HELIX           260..264
FT                   /evidence="ECO:0007829|PDB:6BDX"
SQ   SEQUENCE   269 AA;  28269 MW;  22CFE3A65AD0FDE0 CRC64;
     MIPLKIAIAG ANGRMGRVLV EAVNNHPDTV LSGALEHSGS EALGLDAGYA VGLKTGIAIS
     DDVDAVLAQS DVLIDFTRPE PTLKHLQKCV EKQVNIIIGT TGFDDAGKAA IRAAAEKTGI
     VFAANFSVGV NLTFHILDTV ARVLNEGYDI EIIEGHHRHK VDAPSGTALR MGEVIAGALG
     RDLKQCAVYG REGHTGPRDP STIGFATVRA GDIVGDHTAL FATDGERVEI THKAGSRMTF
     AAGAVRAAVW VNGKTGLYDM QDVLGLNNR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024