ID M0CD91_9EURY Unreviewed; 344 AA.
AC M0CD91;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ELZ19849.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:ELZ19849.1};
GN ORFNames=C476_11629 {ECO:0000313|EMBL:ELZ19849.1};
OS Natrinema limicola JCM 13563.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ19849.1, ECO:0000313|Proteomes:UP000011615};
RN [1] {ECO:0000313|EMBL:ELZ19849.1, ECO:0000313|Proteomes:UP000011615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ19849.1,
RC ECO:0000313|Proteomes:UP000011615};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ19849.1}.
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DR EMBL; AOIT01000041; ELZ19849.1; -; Genomic_DNA.
DR RefSeq; WP_008013060.1; NZ_AOIT01000041.1.
DR AlphaFoldDB; M0CD91; -.
DR STRING; 1230457.C476_11629; -.
DR PATRIC; fig|1230457.4.peg.2341; -.
DR eggNOG; arCOG00494; Archaea.
DR OrthoDB; 38238at2157; -.
DR Proteomes; UP000011615; 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:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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.
PE 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ELZ19849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011615}.
FT DOMAIN 4..131
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 150
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 344 AA; 36720 MW; 923B6520022174F4 CRC64;
MAVRVGVLGA TGAVGQRLIQ LLDPHPDFEI AALTASDASA GKTYRQAAKW RVDSPIPDDV
ADMTVTATDP DDVPNDVDLL FSSLPSSVGE AVEPGFCDAG YVVSSNSSNG RMDEDIPLVI
PEVNAEHLDL LEVQRDERGW DGAMVKNPNC STITFVPTLA ALEEYGLEKV HVATLQAVSG
AGYDGVTSME IIDNAIPHIG GEEDKLETES KKLLGSFDGA ELSLNDVEVG ASCNRIPTID
GHLENVFVET AEDLTPDEAA EAMREYPSLD LYSSPDQLIE VFEDPERPQP RLDRTLGDGM
SIAAGGIRES TFGLQYNCLA HNTMRGAAGA SVLNGELLLE NGYL
//
