ID M0JV34_9EURY Unreviewed; 345 AA.
AC M0JV34;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EMA13007.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:EMA13007.1};
GN Name=asd {ECO:0000313|EMBL:QUJ70674.1};
GN ORFNames=C436_11358 {ECO:0000313|EMBL:EMA13007.1}, KDQ40_08005
GN {ECO:0000313|EMBL:QUJ70674.1};
OS Haloarcula sinaiiensis ATCC 33800.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA13007.1, ECO:0000313|Proteomes:UP000011659};
RN [1] {ECO:0000313|EMBL:EMA13007.1, ECO:0000313|Proteomes:UP000011659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA13007.1,
RC ECO:0000313|Proteomes:UP000011659};
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).
RN [2] {ECO:0000313|EMBL:QUJ70674.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ70674.1};
RA Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT Haloarcula sinaiiensis.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AOLR01000020; EMA13007.1; -; Genomic_DNA.
DR EMBL; CP073366; QUJ70674.1; -; Genomic_DNA.
DR RefSeq; WP_004962544.1; NZ_CP073366.1.
DR AlphaFoldDB; M0JV34; -.
DR GeneID; 64822891; -.
DR KEGG; hsin:KDQ40_08005; -.
DR PATRIC; fig|662476.7.peg.2266; -.
DR OrthoDB; 38238at2157; -.
DR Proteomes; UP000011659; Unassembled WGS sequence.
DR Proteomes; UP000682967; 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: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:EMA13007.1}.
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 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 345 AA; 36718 MW; 866980713AA7730A CRC64;
MTVRVGVLGA TGAVGQRLIQ LLDPHPEFEI AALTASDASV GETYKDAAKW RVNAPIPEDV
AGLEVRATDP DSVPDDVGLI FSSLPSSVGA EVEPEFCEAG YTVSSNSSNA RMDEDVPLII
PEVNADHVDL LEVQRDERGW DGALLKNPNC STITMVPPLA GLDREFDLTD VRVSTLQAVS
GAGYSGVTSM EIIDNAIPHI GGEEQKMESE SRKLLGSFDG AEVQLNEMDV AASCNRIPTL
DGHLENVWAD TAEDISAADA EAAMESVTGI DLPSSPEKLI TVFEEPDRPQ PRLDRNVEDG
MGVAVGGFRE TTDGVQFNCL AHNTMRGAAG ASVLNGELLN KRGYL
//
