ID A0A1F6P1T4_9BACT Unreviewed; 361 AA.
AC A0A1F6P1T4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:OGH90132.1};
GN ORFNames=A2537_03620 {ECO:0000313|EMBL:OGH90132.1};
OS Candidatus Magasanikbacteria bacterium RIFOXYD2_FULL_36_9.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798707 {ECO:0000313|EMBL:OGH90132.1, ECO:0000313|Proteomes:UP000178490};
RN [1] {ECO:0000313|EMBL:OGH90132.1, ECO:0000313|Proteomes:UP000178490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGH90132.1}.
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DR EMBL; MFRC01000007; OGH90132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6P1T4; -.
DR Proteomes; UP000178490; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP 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; 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}.
FT DOMAIN 3..136
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 156
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 361 AA; 39308 MW; CD700680D0F9B3FF CRC64;
MFRVGIIGAT GMVGQRYITL LQGHPWFKVT CVAASANSAG VSYSESVKGR WHMTEPIPKE
VGALTVIDAA NIDQIASACD FVFCAVEMPD KEKVKQLEES LATAGLPVIS SGSAHRFTPD
VPMLLPEINS DHTQMIDIQR KNRGWSKGFI AVKPNCSVQS FLTPIYALRQ AGYEIDRLSV
VTMQAISGAG YPGVPSLDVV DNLVPFIGGE EEKTETEPLK ILGKIKKGKF VLADNLTITA
ACNRVPVSDG HTACVSMSFK KKKPSIEKIL SIWNEFSSVP QKLKLPMAPK QAIIYLNEDN
RPQPKKDRDS EQGMAVSVGR LRECPVFDYK FVGLSHNTIR GAAGGGILNA ELLVKQGYIT
K
//
