ID A0A1G1ZLB5_9BACT Unreviewed; 375 AA.
AC A0A1G1ZLB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:OGY65305.1};
GN ORFNames=A3A16_01845 {ECO:0000313|EMBL:OGY65305.1};
OS Candidatus Harrisonbacteria bacterium RIFCSPLOWO2_01_FULL_44_18.
OC Bacteria; Candidatus Harrisonbacteria.
OX NCBI_TaxID=1798407 {ECO:0000313|EMBL:OGY65305.1, ECO:0000313|Proteomes:UP000177942};
RN [1] {ECO:0000313|EMBL:OGY65305.1, ECO:0000313|Proteomes:UP000177942}
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:OGY65305.1}.
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; MHJJ01000012; OGY65305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ZLB5; -.
DR STRING; 1798407.A3A16_01845; -.
DR Proteomes; UP000177942; 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; 2.
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 6..153
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 172
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 375 AA; 40996 MW; 9F8FB93E9F345E12 CRC64;
MERKLKVGIL GATGTVGQKF IILLQNHPWF EITALAASSE SAGKTYEKAV AGRWKQEVDI
PANVRKMTVL ECDPAKFNSH GRVRIAGASR GEGARFGCCD FVFSGLDASA AGEIEKSFAA
AGYPVISNAK NFRMDADVPL LVPEVNADHA AIIPFQQKRR NWKGFIVTNP NCVVVPLAMA
LKPIHQKYGV SKVMVTSMQA VSGAGYPGVA SLDILDNIIP YISGEEPKVE TEPLKLLGEM
KKNAFRFAKI KISAQCNRVP TKDGHFLTVA FATKKPAKVG DIKKLIKKFK GEPQKMKLPS
APKRPLVYLE DDFRPQVRFD RDREGGMAVS IGRLREDPVL GFKMVVLGHN TIRGAAGAAI
LNAELLYKKG HLRTK
//
