ID E3BDL1_9MICO Unreviewed; 362 AA.
AC E3BDL1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EFP56869.1};
GN ORFNames=HMPREF0321_0702 {ECO:0000313|EMBL:EFP56869.1};
OS Dermacoccus sp. Ellin185.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Dermacoccus.
OX NCBI_TaxID=188626 {ECO:0000313|EMBL:EFP56869.1, ECO:0000313|Proteomes:UP000003057};
RN [1] {ECO:0000313|EMBL:EFP56869.1, ECO:0000313|Proteomes:UP000003057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin185 {ECO:0000313|EMBL:EFP56869.1,
RC ECO:0000313|Proteomes:UP000003057};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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:EFP56869.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEIQ01000117; EFP56869.1; -; Genomic_DNA.
DR RefSeq; WP_006947187.1; NZ_AEIQ01000117.1.
DR AlphaFoldDB; E3BDL1; -.
DR eggNOG; COG0136; Bacteria.
DR Proteomes; UP000003057; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 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 3: Inferred from homology;
FT DOMAIN 10..125
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
SQ SEQUENCE 362 AA; 38544 MW; 284271B0D6DA4279 CRC64;
MTANQPERPV LAVVGPTGLV GQAVIDVLAT RADAWDDVRL FGSDRSVGRR MLFGVDEIEV
EPLDSESFAG VDVAIFATPA DVSAKWAPFA TASDCLVVDT SAAFRDDDDV PLVVPEVNAA
AAFEHPRGIV AMPSGPAIVM LPVLATLHEH WSLTHVTATS MQAVTGAGKR GAERLYEEVS
ALTGHPRIGQ MPGDVRRYVA DLPDDSPFPA PIVSNVVPWV GEHVGGGWSS EENDIAHELR
DVLALPQLRV AVTCVQVPIV TTHMSTLHVS FDKKVKPDDA RRAIVEGANG AIVMPDENGT
DWPTPADAVG TDPVWVGRVR QVESNPHTLD FIVCGDNIRK GAALNALQIA EMLVGVGRYA
QA
//
