ID D3APX7_9CLOT Unreviewed; 362 AA.
AC D3APX7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EFC96126.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:EFC96126.1};
GN Name=asd {ECO:0000313|EMBL:EFC96126.1};
GN ORFNames=CLOSTHATH_05681 {ECO:0000313|EMBL:EFC96126.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC96126.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFC96126.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC96126.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) 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:EFC96126.1}.
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DR EMBL; ACIO01000615; EFC96126.1; -; Genomic_DNA.
DR RefSeq; WP_006776101.1; NZ_GG667768.1.
DR AlphaFoldDB; D3APX7; -.
DR HOGENOM; CLU_049966_1_0_9; -.
DR Proteomes; UP000004968; 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:EFC96126.1}.
FT DOMAIN 6..138
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 158
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 362 AA; 40411 MW; 218ED622C3BC7D38 CRC64;
MEKKLKVGVL GATGMVGQRF ISLLENHPWY EVVTMAASPR SAGKTYEEAV GDRWKMTTPM
PEAVKKLTVM NVNEVEKVAA SVDFVFSAVD MTKEEIKAIE EAYAKTETPV VSNNSAHRWT
PDVPMVVPEI NPEHFEVIKD QRKRLGTERG FIAVKPNCSI QSYAPVLTAW KEFEPYEVVA
TTYQAISGAG KTFKDWPEME GNIIPYIGGE EEKSEQEPLR LWGKVENGEI VKANEPVITC
QCIRVPVLNG HTAAVFVKFR KKPTKEELIE RLVSFKGLPQ ELELPSAPKQ FIQYLNEDNR
PQVTMDVDFE HGMGVSIGRL REDTVYDYKF VGLSHNTVRG AAGGAVLCAE LLTAQGYIQA
KS
//
