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Database: UniProt
Entry: A0A0S7WGJ0_9CHLR
LinkDB: A0A0S7WGJ0_9CHLR
Original site: A0A0S7WGJ0_9CHLR 
ID   A0A0S7WGJ0_9CHLR        Unreviewed;       353 AA.
AC   A0A0S7WGJ0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE            EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN   ORFNames=AMJ38_03770 {ECO:0000313|EMBL:KPJ49215.1};
OS   Dehalococcoidia bacterium DG_22.
OC   Bacteria; Chloroflexota; Dehalococcoidia.
OX   NCBI_TaxID=1703393 {ECO:0000313|EMBL:KPJ49215.1, ECO:0000313|Proteomes:UP000054105};
RN   [1] {ECO:0000313|EMBL:KPJ49215.1, ECO:0000313|Proteomes:UP000054105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_22 {ECO:0000313|EMBL:KPJ49215.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010584}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPJ49215.1}.
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DR   EMBL; LIZQ01000080; KPJ49215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7WGJ0; -.
DR   PATRIC; fig|1703393.3.peg.689; -.
DR   Proteomes; UP000054105; Unassembled WGS sequence.
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:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   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.
PE   3: Inferred from homology;
FT   DOMAIN          4..119
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        128
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        244
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   353 AA;  38557 MW;  CA9705347E11C55D CRC64;
     MALKVTVVGV GMVGEQIVSI LRERGFPMQW PPRICATRAR SETLAGEGFH VEETADEAFE
     GADVVFFAGK EGGKGASVQW GKKAVEAGAI CVDNGGDFRM DPAVPLVVPE VNLDAVTPDK
     SFIASPNCST IQMVLVLDAL HRAAKIRRVV VSTYQSVSGW GVAAQEDLLA QIPHALKSLD
     DIPFEPTVFA SPIAFNLFPH IDKFTEDGYT KEEMKMVWET QKIMGDDTIK ISPTTVRVPV
     LVGHGEALNI ETERKLTPAE AREILASSPG IVVIDEPNIN TPRNDPLERT YPVPLDVRKP
     EYQDMVLVGR IREDPTIENG LNLWCVSDNL RKGAALNVVQ IAEGLIERGR LNP
//
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