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Database: UniProt
Entry: Q0W684_METAR
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Original site: Q0W684_METAR 
ID   Q0W684_METAR            Unreviewed;       344 AA.
AC   Q0W684;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE            EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN   Name=asd {ECO:0000313|EMBL:CAJ36109.1};
GN   ORFNames=RCIX722 {ECO:0000313|EMBL:CAJ36109.1};
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160 {ECO:0000313|EMBL:CAJ36109.1, ECO:0000313|Proteomes:UP000000663};
RN   [1] {ECO:0000313|EMBL:CAJ36109.1, ECO:0000313|Proteomes:UP000000663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50
RC   {ECO:0000313|Proteomes:UP000000663};
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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; AM114193; CAJ36109.1; -; Genomic_DNA.
DR   RefSeq; WP_012036400.1; NC_009464.1.
DR   AlphaFoldDB; Q0W684; -.
DR   STRING; 351160.RCIX722; -.
DR   GeneID; 5142964; -.
DR   KEGG; rci:RCIX722; -.
DR   PATRIC; fig|351160.9.peg.2132; -.
DR   eggNOG; arCOG00494; Archaea.
DR   OrthoDB; 38238at2157; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000000663; Chromosome.
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; IPR005676; Asp_semi-ald_DH_pep-lack.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   NCBIfam; TIGR00978; asd_EA; 1.
DR   PANTHER; PTHR46718; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR46718:SF1; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 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   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAJ36109.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000663}.
FT   DOMAIN          3..128
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        147
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   344 AA;  37660 MW;  C9671A5DBFC2C4D2 CRC64;
     MIKVGILGAT GNVGQRFIQQ LAGHPWFEIT ALAASERSAG KPYEQVAKWR LDTDLPEEVR
     ELTVVPTKPE AVDADLVFSA LPAEDAIKIE ADFAKAGMVV CSNASAHRME KDVPLVIPEV
     NPEHLGLIDV QRKKRKWDGA IVTNPNCSTI MMVVTLKPLM KFGIENIHVS TMQAVSGAGY
     EGVPSMAIID NMIPYIGSEE GKMETETLKL LGDFDGKQVK EAPFWVSAAC HRVGVLDGHT
     MSIWARFNKK VTPEKVKDAF LKFDPKLSDL PTSPKKAIIV REEPDRPQPR MDRMQGNGMS
     ISVGRIRAGK ADSIQYVCMG HNTIRGAAGA SVLNAELLKK KGYL
//
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