DHAS_METJA
ID DHAS_METJA Reviewed; 354 AA.
AC Q57658;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121};
DE EC=1.2.1.11;
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=MJ0205;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION,
RP CATALYTIC ACTIVITY, COENZYME SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP DOMAIN, AND SUBUNIT.
RX PubMed=16225889; DOI=10.1016/j.jmb.2005.09.027;
RA Faehnle C.R., Ohren J.F., Viola R.E.;
RT "A new branch in the family: structure of aspartate-beta-semialdehyde
RT dehydrogenase from Methanococcus jannaschii.";
RL J. Mol. Biol. 353:1055-1068(2005).
CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-
CC 4-phosphate. To a lesser extent, is able to use NAD instead of NADP.
CC {ECO:0000269|PubMed:16225889}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC Evidence={ECO:0000269|PubMed:16225889};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for NADP(+) {ECO:0000269|PubMed:16225889};
CC KM=1700 uM for NAD(+) {ECO:0000269|PubMed:16225889};
CC Note=kcat is 4 sec(-1) for the L-4-aspartyl-phosphate-forming
CC reaction (at 70 degrees Celsius).;
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:16225889};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_02121}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16225889}.
CC -!- DOMAIN: Consists of two domains, an N-terminal nucleotide-binding
CC domain and a C-terminal dimerization domain.
CC {ECO:0000269|PubMed:16225889}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_02121}.
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DR EMBL; L77117; AAB98189.1; -; Genomic_DNA.
DR PIR; F64325; F64325.
DR PDB; 1YS4; X-ray; 2.29 A; A/B=1-354.
DR PDBsum; 1YS4; -.
DR AlphaFoldDB; Q57658; -.
DR SMR; Q57658; -.
DR STRING; 243232.MJ_0205; -.
DR EnsemblBacteria; AAB98189; AAB98189; MJ_0205.
DR KEGG; mja:MJ_0205; -.
DR eggNOG; arCOG00494; Archaea.
DR HOGENOM; CLU_049966_1_0_2; -.
DR InParanoid; Q57658; -.
DR OMA; WPEMVDN; -.
DR PhylomeDB; Q57658; -.
DR BioCyc; MetaCyc:MON-20453; -.
DR SABIO-RK; Q57658; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR EvolutionaryTrace; Q57658; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_02121; ASADH; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR InterPro; IPR012080; Asp_semialdehyde_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00978; asd_EA; 1.
DR PROSITE; PS01103; ASD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW Lysine biosynthesis; Methionine biosynthesis; NAD; NADP; Oxidoreductase;
KW Reference proteome; Threonine biosynthesis.
FT CHAIN 1..354
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141397"
FT ACT_SITE 157
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:16225889"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16225889"
FT BINDING 17..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16225889"
FT BINDING 42..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16225889"
FT BINDING 118
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 187..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16225889"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 213
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 333..334
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16225889"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:1YS4"
FT STRAND 321..331
FT /evidence="ECO:0007829|PDB:1YS4"
FT TURN 333..338
FT /evidence="ECO:0007829|PDB:1YS4"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:1YS4"
SQ SEQUENCE 354 AA; 39439 MW; 5C412CA5C39B166E CRC64;
MSKGEKMKIK VGVLGATGSV GQRFVQLLAD HPMFELTALA ASERSAGKKY KDACYWFQDR
DIPENIKDMV VIPTDPKHEE FEDVDIVFSA LPSDLAKKFE PEFAKEGKLI FSNASAYRME
EDVPLVIPEV NADHLELIEI QREKRGWDGA IITNPNCSTI CAVITLKPIM DKFGLEAVFI
ATMQAVSGAG YNGVPSMAIL DNLIPFIKNE EEKMQTESLK LLGTLKDGKV ELANFKISAS
CNRVAVIDGH TESIFVKTKE GAEPEEIKEV MDKFDPLKDL NLPTYAKPIV IREEIDRPQP
RLDRNEGNGM SIVVGRIRKD PIFDVKYTAL EHNTIRGAAG ASVLNAEYFV KKYI
