DHAS2_VIBCH
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 03-AUG-2022, entry version 161.
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; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC 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 + 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: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};
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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; NP_231739.1; NC_002505.1.
DR RefSeq; WP_000082625.1; NZ_LT906614.1.
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 PDBsum; 2QZ9; -.
DR PDBsum; 2R00; -.
DR AlphaFoldDB; P23247; -.
DR SMR; P23247; -.
DR STRING; 243277.VC_2107; -.
DR DNASU; 2613363; -.
DR EnsemblBacteria; AAF95253; AAF95253; VC_2107.
DR GeneID; 57740728; -.
DR KEGG; vch:VC_2107; -.
DR PATRIC; fig|243277.26.peg.2013; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_0_1_6; -.
DR OMA; CEEEMKM; -.
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 1.
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; 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 Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01296; asd_B; 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..11
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 125..128
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 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
