ID DHAS2_VIBCH Reviewed; 337 AA. AC P23247; O34226; Q9KQ93; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 02-SEP-2026, entry version 174. DE RecName: Full=Aspartate-semialdehyde dehydrogenase 2; DE Short=ASA dehydrogenase 2; DE Short=ASADH 2; DE EC=1.2.1.11 {ECO:0000269|PubMed:12071715}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase 2; GN Name=asd2; Synonyms=asd; OrderedLocusNames=VC_2107; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CDV 101; RA Avest A.R., Frits R.M.; RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=El Tor C7258 / Serotype O1; RA Fando R., Benitez J.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=12071715; DOI=10.1006/prep.2002.1626; RA Moore R.A., Bocik W.E., Viola R.E.; RT "Expression and purification of aspartate beta-semialdehyde dehydrogenase RT from infectious microorganisms."; RL Protein Expr. Purif. 25:189-194(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH RP L-ASPARTATE-SEMIALDEHYDE, SUBUNIT, AND DOMAIN. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=18323627; DOI=10.1107/s0907444907068552; RA Viola R.E., Liu X., Ohren J.F., Faehnle C.R.; RT "The structure of a redundant enzyme: a second isoform of aspartate beta- RT semialdehyde dehydrogenase in Vibrio cholerae."; RL Acta Crystallogr. D 64:321-330(2008). 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:0000269|PubMed:12071715}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate 4-semialdehyde + phosphate + NADP(+) = 4-phospho- CC L-aspartate + NADPH + H(+); 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:12071715}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.16 mM for L-aspartate 4-semialdehyde CC {ECO:0000269|PubMed:12071715}; CC KM=0.36 mM for NADP(+) {ECO:0000269|PubMed:12071715}; CC KM=22 mM for phosphate {ECO:0000269|PubMed:12071715}; 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:0000255|HAMAP-Rule:MF_02121, CC ECO:0000305|PubMed:18323627}. CC -!- DOMAIN: Consists of two domains, an N-terminal nucleotide-binding CC domain and a C-terminal dimerization domain. CC {ECO:0000269|PubMed:18323627}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF95253.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; X55363; CAA39048.1; -; Genomic_DNA. DR EMBL; Y15281; CAA75569.1; -; Genomic_DNA. DR EMBL; AE003852; AAF95253.1; ALT_INIT; Genomic_DNA. DR PIR; B82118; B82118. DR PIR; S14523; S14523. DR RefSeq; WP_000082625.1; NC_002505.1. DR PDB; 2QZ9; X-ray; 2.20 A; A/B/C=2-337. DR PDB; 2R00; X-ray; 2.03 A; A/B/C=2-337. DR AlphaFoldDB; P23247; -. DR SMR; P23247; -. DR STRING; 243277.VC_2107; -. DR DNASU; 2613363; -. DR EnsemblBacteria; AAF95253; AAF95253; VC_2107. DR KEGG; vch:VC_2107; -. DR PATRIC; fig|243277.26.peg.2013; -. DR eggNOG; COG0136; Bacteria. DR HOGENOM; CLU_049966_0_1_6; -. DR BRENDA; 1.2.1.11; 6626. DR SABIO-RK; P23247; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR EvolutionaryTrace; P23247; -. DR Proteomes; UP000000584; Chromosome I. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; EXP:UniProtKB. 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:0009090; P:L-homoserine biosynthetic process; IBA:GO_Central. DR GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd18131; ASADH_C_bac_euk_like; 1. DR CDD; cd02316; VcASADH2_like_N; 1. DR FunFam; 3.40.50.720:FF:000099; Aspartate-semialdehyde dehydrogenase; 1. DR FunFam; 3.30.360.10:FF:000054; Aspartate-semialdehyde dehydrogenase 2; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR NCBIfam; TIGR01296; asd_B; 1. DR NCBIfam; NF004224; PRK05671.1; 1. DR NCBIfam; NF005957; PRK08040.1; 1. DR NCBIfam; NF011456; PRK14874.1; 1. DR PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; NADP; Oxidoreductase; KW Reference proteome; Threonine biosynthesis. FT CHAIN 1..337 FT /note="Aspartate-semialdehyde dehydrogenase 2" FT /id="PRO_0000141394" FT ACT_SITE 132 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000269|PubMed:18323627" FT ACT_SITE 245 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 13..16 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 41..42 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 101 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 162..163 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 216 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 316 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT VARIANT 40 FT /note="E -> D (in strain: C7258)" FT CONFLICT 188..189 FT /note="NT -> QA (in Ref. 1; CAA39048)" FT /evidence="ECO:0000305" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:2R00" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 15..26 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:2R00" FT TURN 40..44 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 46..49 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 76..88 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:2R00" FT TURN 99..102 FT /evidence="ECO:0007829|PDB:2R00" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 115..123 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 132..148 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 150..163 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 165..180 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:2QZ9" FT HELIX 188..191 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:2R00" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 212..224 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 231..241 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 243..255 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 259..268 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 272..274 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 293..301 FT /evidence="ECO:0007829|PDB:2R00" FT STRAND 304..316 FT /evidence="ECO:0007829|PDB:2R00" FT HELIX 317..336 FT /evidence="ECO:0007829|PDB:2R00" SQ SEQUENCE 337 AA; 37375 MW; 143D7E55593308FD CRC64; MSQQFNVAIF GATGAVGETM LEVLQEREFP VDELFLLASE RSEGKTYRFN GKTVRVQNVE EFDWSQVHIA LFSAGGELSA KWAPIAAEAG VVVIDNTSHF RYDYDIPLVV PEVNPEAIAE FRNRNIIANP NCSTIQMLVA LKPIYDAVGI ERINVTTYQS VSGAGKAGID ELAGQTAKLL NGYPAETNTF SQQIAFNCIP QIDQFMDNGY TKEEMKMVWE TQKIFNDPSI MVNPTCVRVP VFYGHAEAVH VETRAPIDAE QVMDMLEQTD GIELFRGADF PTQVRDAGGK DHVLVGRVRN DISHHSGINL WVVADNVRKG AATNAVQIAE LLVRDYF //