ID C6LEF0_9FIRM Unreviewed; 371 AA.
AC C6LEF0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EET60933.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:EET60933.1};
GN Name=asd {ECO:0000313|EMBL:EET60933.1};
GN ORFNames=BRYFOR_06999 {ECO:0000313|EMBL:EET60933.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET60933.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET60933.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET60933.1,
RC ECO:0000313|Proteomes:UP000005561};
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 (JUL-2009) 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:EET60933.1}.
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DR EMBL; ACCL02000008; EET60933.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LEF0; -.
DR STRING; 168384.SAMN05660368_00387; -.
DR eggNOG; COG0136; Bacteria.
DR Proteomes; UP000005561; 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:EET60933.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005561}.
FT DOMAIN 11..143
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 163
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 371 AA; 41364 MW; 31B6E082694A50C8 CRC64;
MEEKIMNEKL RVGILGATGM VGQRFISLLE NHPWFEVTTV AASPRSAGKT YEEAVGGRWK
MTTPMPEAVK KLVVMNVNEV EKVAAGVDFV FSAVDMTKDE IRAIEEEYAK TETPVVSNNS
AHRWTPDVPM VIPEINPEHF KVIEFQKKRL GTTRGFVAVK PNCSIQSYAP ALAAWKEFEP
YEVVATTYQA ISGAGKTFKD WPEMVENIIP YIGGEEEKSE QEPLRILGEL KDGVIVKAQE
PVITCQCIRV PVLNGHTAAV FVKFRKKPTK EQLIEKLVNF SGLPQELHLP SAPKQFIQYM
EEDNRPQVKA DVDYEKGMGV SIGRLREDTV YDYKFVGLSH NTVRGAAGGA VLCAECLKAL
GYIDRKSNTP L
//
