ID A0A0P7I4W2_9EURY Unreviewed; 344 AA.
AC A0A0P7I4W2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KPN32008.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:KPN32008.1};
GN Name=asd {ECO:0000313|EMBL:KPN32008.1};
GN ORFNames=SY89_02765 {ECO:0000313|EMBL:KPN32008.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN32008.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:KPN32008.1}.
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DR EMBL; LGUC01000001; KPN32008.1; -; Genomic_DNA.
DR RefSeq; WP_054584399.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7I4W2; -.
DR STRING; 699431.SY89_02765; -.
DR PATRIC; fig|699431.3.peg.2828; -.
DR OrthoDB; 38238at2157; -.
DR Proteomes; UP000050535; 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:KPN32008.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535}.
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; 36881 MW; C107596FB4048022 CRC64;
MTVRVGLLGA TGAVGQRFVQ LLDDHPTFEI AAVTASPESA GESYRDAAKW RVDTPIPERI
AELTVRETSP DALPDDLDLL FSSLPSSVGA EIEPELCRAG YVVSSNSSNE RMAEDVPLTI
PEVNPDHLDL IDTQREQRGW DGALVKNPNC STITMTPTLA ALDEFGLERA HVSTLQAVSG
AGYSGVTSME IIDNVLPHIG GEEEKMETES RKLLGDVEDG ELSLHDVDVS ASCNRVPSLD
GHLENVFAEL DDDPSADAVH EALANFEAVD LPSAPAQPIH VFDDPERPQP RLDRMRGKGM
QISAGGLQAT DEGVQYNCLA HNTIRGAAGA SVLNGELLVE EGWV
//