DHAS_NEIMB
ID DHAS_NEIMB Reviewed; 371 AA.
AC P30903;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 {ECO:0000255|HAMAP-Rule:MF_02121};
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=NMB2079;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140.
RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a;
RX PubMed=8101504; DOI=10.1016/0378-1119(93)90707-a;
RA Hatten L., Wang L., Schryvers A.B., Schweizer H.P.;
RT "Cloning and characterization of the Neisseria meningitidis asd gene.";
RL Gene 129:123-128(1993).
CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-
CC 4-phosphate. {ECO:0000255|HAMAP-Rule:MF_02121}.
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:0000255|HAMAP-Rule:MF_02121};
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.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_02121}.
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DR EMBL; AE002098; AAF42397.1; -; Genomic_DNA.
DR EMBL; Z14063; CAA78444.1; -; Genomic_DNA.
DR PIR; E81009; E81009.
DR RefSeq; NP_275068.1; NC_003112.2.
DR RefSeq; WP_002225714.1; NC_003112.2.
DR AlphaFoldDB; P30903; -.
DR SMR; P30903; -.
DR STRING; 122586.NMB2079; -.
DR PaxDb; P30903; -.
DR EnsemblBacteria; AAF42397; AAF42397; NMB2079.
DR KEGG; nme:NMB2079; -.
DR PATRIC; fig|122586.8.peg.2660; -.
DR HOGENOM; CLU_066397_0_0_4; -.
DR OMA; MFDVPDE; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
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:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02121; ASADH; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR InterPro; IPR011534; Asp_ADH_gamma-type.
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 PANTHER; PTHR46278:SF4; PTHR46278:SF4; 1.
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; TIGR01745; asd_gamma; 1.
DR PROSITE; PS01103; ASD; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis;
KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..371
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141385"
FT ACT_SITE 135
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 73
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 102
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 165..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 244
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT CONFLICT 44
FT /note="A -> R (in Ref. 2; CAA78444)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..119
FT /note="DVL -> NVI (in Ref. 2; CAA78444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 39858 MW; F36BF70BB80075AA CRC64;
MKVGFVGWRG MVGSVLMQRM KEENDFAHIP EAFFFTTSNV GGAAPDFGQA AKTLLDANNV
AELAKMDIIV TCQGGDYTKS VFQALRDSGW NGYWIDAASS LRMKDDAIIV LDPVNRDVLD
NGLKNGVKNY IGGNCTVSLM LMALGGLFQN DLVEWATSMT YQAASGAGAK NMRELISGMG
AVHAQVADAL ADPAGSILDI DRKVSDFLRS EDYPKANFGV PLAGSLIPWI DVDLGNGQSK
EEWKGGVETN KILGRSDNPT VIDGLCVRVG AMRCHSQAIT LKLKKDLPVS EIETILAGAN
DWVKVIPNEK EASIHELTPA KVTGTLSVPV GRIRKLGMGG EYISAFTVGD QLLWGAAEPL
RRVLRIVLGS L
