ID Q6XVF0_CAMJU Unreviewed; 188 AA.
AC Q6XVF0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 13-SEP-2023, entry version 70.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
DE Flags: Fragment;
GN Name=asd {ECO:0000313|EMBL:AAP41859.1};
OS Campylobacter jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197 {ECO:0000313|EMBL:AAP41859.1};
RN [1] {ECO:0000313|EMBL:AAP41859.1}
RP NUCLEOTIDE SEQUENCE.
RA Sails A.D., Suerbaum S., Swaminathan B., Fields P.I.;
RT "A comparison of two multilocus sequence typing methods for characterizing
RT Campylobacter jejuni.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001636};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00005076}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005021}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; AY207090; AAP41859.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6XVF0; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
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: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 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 3: Inferred from homology;
FT DOMAIN 3..36
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01118"
FT DOMAIN 57..187
FT /note="Semialdehyde dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02774"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP41859.1"
FT NON_TER 188
FT /evidence="ECO:0000313|EMBL:AAP41859.1"
SQ SEQUENCE 188 AA; 21267 MW; C93CDEF295EA29D3 CRC64;
FAVESSAVVI DNTSHFRMEK DVPLVVPECN PEDIKDWKKT GIIANPNCST IQMVQVLKPL
NDAFNLKRVD VSTYQAASGA GKEGMQELVE AMQSFFAFKL DEFKSQTFPY TLALNLIPQI
DVFMDNDYTK EELKMVNETQ KILHKNLEVS ATCVRVPVLR SHSEAITMHF EKEIDVKKAK
EILEKAPS
//
