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ASPD_THEMA
ID   ASPD_THEMA              Reviewed;         241 AA.
AC   Q9X1X6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=L-aspartate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000305};
DE            EC=1.4.1.21 {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:12496312};
GN   Name=nadX {ECO:0000255|HAMAP-Rule:MF_01265}; OrderedLocusNames=TM_1643;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD.
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga
RT   maritima at 1.9 A resolution.";
RL   Submitted (JUL-2002) to the PDB data bank.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-241 IN COMPLEX WITH NAD,
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=12496312; DOI=10.1074/jbc.m211892200;
RA   Yang Z., Savchenko A., Yakunin A.F., Zhang R., Edwards A.M.,
RA   Arrowsmith C.H., Tong L.;
RT   "Aspartate dehydrogenase, a novel enzyme identified from structural and
RT   functional studies of TM1643.";
RL   J. Biol. Chem. 278:8804-8808(2003).
CC   -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC       dehydrogenation of L-aspartate to iminoaspartate. Does not show
CC       aspartate oxidase activity. Is also able to catalyze the reverse
CC       reaction, i.e. the reductive amination of oxaloacetate.
CC       {ECO:0000269|PubMed:12496312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11784, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01265,
CC         ECO:0000269|PubMed:12496312};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11788, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01265,
CC         ECO:0000269|PubMed:12496312};
CC   -!- ACTIVITY REGULATION: Competitively inhibited by L-malate and NH(4)(+).
CC       {ECO:0000269|PubMed:12496312}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.067 mM for L-aspartate (in the presence of NAD)
CC         {ECO:0000269|PubMed:12496312};
CC         KM=1.20 mM for L-aspartate (in the presence of NADP)
CC         {ECO:0000269|PubMed:12496312};
CC         KM=0.25 mM for NAD {ECO:0000269|PubMed:12496312};
CC         KM=0.72 mM for NADP {ECO:0000269|PubMed:12496312};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01265}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12496312}.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia.
CC       {ECO:0000255|HAMAP-Rule:MF_01265}.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000305}.
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DR   EMBL; AE000512; AAD36710.1; -; Genomic_DNA.
DR   PIR; H72226; H72226.
DR   RefSeq; NP_229443.1; NC_000853.1.
DR   RefSeq; WP_004082138.1; NZ_CP011107.1.
DR   PDB; 1H2H; X-ray; 2.60 A; A=1-241.
DR   PDB; 1J5P; X-ray; 1.90 A; A=1-241.
DR   PDBsum; 1H2H; -.
DR   PDBsum; 1J5P; -.
DR   AlphaFoldDB; Q9X1X6; -.
DR   SMR; Q9X1X6; -.
DR   STRING; 243274.THEMA_06030; -.
DR   EnsemblBacteria; AAD36710; AAD36710; TM_1643.
DR   KEGG; tma:TM1643; -.
DR   eggNOG; COG1712; Bacteria.
DR   InParanoid; Q9X1X6; -.
DR   OMA; ECAGHSA; -.
DR   OrthoDB; 1670363at2; -.
DR   BRENDA; 1.4.1.21; 6331.
DR   SABIO-RK; Q9X1X6; -.
DR   UniPathway; UPA00253; UER00456.
DR   EvolutionaryTrace; Q9X1X6; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; 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:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01265; NadX; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR022487; Asp_DH_arc.
DR   InterPro; IPR020626; Asp_DH_prok.
DR   InterPro; IPR011182; L-Asp_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01958; DUF108; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03855; NAD_NadX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..241
FT                   /note="L-aspartate dehydrogenase"
FT                   /id="PRO_0000144893"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT                   ECO:0000305|PubMed:12496312"
FT   BINDING         10..11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   BINDING         28
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   BINDING         56..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   BINDING         63..64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   BINDING         78..79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   BINDING         109
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT                   ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   BINDING         164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT                   ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT                   ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           10..18
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          22..27
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           58..68
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           80..84
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           86..97
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           113..119
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           134..137
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           152..158
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           164..173
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          192..201
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:1J5P"
FT   HELIX           221..235
FT                   /evidence="ECO:0007829|PDB:1J5P"
SQ   SEQUENCE   241 AA;  26640 MW;  AF52221512C3DE2E CRC64;
     MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL DEFQVPSDVS TVVECASPEA
     VKEYSLQILK NPVNYIIIST SAFADEVFRE RFFSELKNSP ARVFFPSGAI GGLDVLSSIK
     DFVKNVRIET IKPPKSLGLD LKGKTVVFEG SVEEASKLFP RNINVASTIG LIVGFEKVKV
     TIVADPAMDH NIHIVRISSA IGNYEFKIEN IPSPENPKTS MLTVYSILRT LRNLESKIIF
     G
 
 
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