ID D6PJJ2_9BACT Unreviewed; 173 AA.
AC D6PJJ2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=Semialdehyde dehydrogenase dimerisation domain-containing protein {ECO:0000259|Pfam:PF02774};
OS uncultured marine bacterium MedDCM-OCT-S08-C1068.
OC Bacteria; environmental samples.
OX NCBI_TaxID=743068 {ECO:0000313|EMBL:ADD95893.1};
RN [1] {ECO:0000313|EMBL:ADD95893.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20393571; DOI=10.1038/ismej.2010.44;
RA Ghai R., Martin-Cuadrado A.B., Molto A.G., Heredia I.G., Cabrera R.,
RA Martin J., Verdu M., Deschamps P., Moreira D., Lopez-Garcia P., Mira A.,
RA Rodriguez-Valera F.;
RT "Metagenome of the Mediterranean deep chlorophyll maximum studied by direct
RT and fosmid library 454 pyrosequencing.";
RL ISME J. 4:1154-1166(2010).
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DR EMBL; GU943108; ADD95893.1; -; Genomic_DNA.
DR AlphaFoldDB; D6PJJ2; -.
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; IPR012280; Semialdhyde_DH_dimer_dom.
DR PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
PE 4: Predicted;
FT DOMAIN 1..151
FT /note="Semialdehyde dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02774"
SQ SEQUENCE 173 AA; 19618 MW; 55FD22C58EB0E427 CRC64;
MDELIEQTKQ VLQNNKVESK NFTKQIAFNA IPHIDVFTDD GYTKEELKMT NETKKILDND
IDLTATCVRL PVLVSHSESV NIEFEKSFTL EKVRKALDNF EGCKVIDERV NGGYSTPLEA
EGKDETFISR IRKDKTVTNG LNMWIVSDNL LRGAALNAVE IAETLIKNNF YGK
//