ID A0A0P6WR19_9CHLR Unreviewed; 351 AA.
AC A0A0P6WR19;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KPL71328.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:KPL71328.1};
GN ORFNames=ADM99_11560 {ECO:0000313|EMBL:KPL71328.1};
OS Leptolinea tardivitalis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Leptolinea.
OX NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL71328.1, ECO:0000313|Proteomes:UP000050430};
RN [1] {ECO:0000313|EMBL:KPL71328.1, ECO:0000313|Proteomes:UP000050430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL71328.1,
RC ECO:0000313|Proteomes:UP000050430};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL Submitted (JUL-2015) 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:KPL71328.1}.
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DR EMBL; LGCK01000011; KPL71328.1; -; Genomic_DNA.
DR RefSeq; WP_062423452.1; NZ_LGCK01000011.1.
DR AlphaFoldDB; A0A0P6WR19; -.
DR STRING; 229920.ADM99_11560; -.
DR PATRIC; fig|229920.5.peg.3519; -.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000050430; 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:KPL71328.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050430}.
FT DOMAIN 6..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 351 AA; 38066 MW; 95B750350EE3AA48 CRC64;
MNKKIPVAIL GANGSVGQRF IQLLENHPWF EVKCLTGSDR SIGKPYAQTC HWILPERMPD
AVKGMILKEN EEAVKDCQVA FSAMPADQAK EVEVELAASG MAVVSNASSH RMDPDVPILL
PEVNPDHTAL VNIQRKKHKW KGFIVTNPNC TSTGMTVSLK PLLDAFGIEQ VIAVSLQALS
GAGYPGVASM DIIDNVVPYI KGEEEKVESE PLKMLGNLSD DHIQNAGFVI SAHTNRVAVT
DGHTVCVSIK TGRNVKPEDA IEVMRSYTCP EISRELPSSP WPVIAVHDAP DRPQPRLDRA
IGGGMTTSVG RMRIDPIMGL KYIVLSHNTV RGAAGGAVFN AELLVQQKLI D
//
