ID A0A136L3F0_9CHLR Unreviewed; 369 AA.
AC A0A136L3F0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KXK16066.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:KXK16066.1};
GN Name=asd {ECO:0000313|EMBL:KXK16066.1};
GN ORFNames=UZ14_CFX002000102 {ECO:0000313|EMBL:KXK16066.1};
OS Chloroflexi bacterium OLB14.
OC Bacteria; Chloroflexota; Tepidiformia.
OX NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK16066.1, ECO:0000313|Proteomes:UP000070321};
RN [1] {ECO:0000313|EMBL:KXK16066.1, ECO:0000313|Proteomes:UP000070321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB14 {ECO:0000313|EMBL:KXK16066.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK16066.1}.
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DR EMBL; LMZR01000005; KXK16066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136L3F0; -.
DR STRING; 1617415.UZ14_CFX002000102; -.
DR PATRIC; fig|1617415.3.peg.105; -.
DR Proteomes; UP000070321; 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: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; 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:KXK16066.1}.
FT DOMAIN 5..130
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 149
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 369 AA; 39669 MW; 6B3155F29BCD30B7 CRC64;
MNQIPVAVLG ATGSVGQRFI SLLENHPWFK VVALAASDRS VNQKYSQATR WILDSPMPDY
AKDMIIVPAS VEAVQAKIVF SALHSDVAKE LEPQFAKAGV AVCSNASAFR QADDVPLLLP
EVNANHIHLI TTQRKNKNWS GCIITNPNCT STGLTVALKA LDDAFGVKKV FAVSMQALSG
AGYPGVSSMD IIDNIIPNIN GEEEKVELEP RKMLGKYIES LVPPSSAGYD SAAGTPPRAF
IEFADIKFSA HTNRVAVLDG HTVCASVALS TPQPDLQVVS DILRNYSAPE SAKNLPSSPR
PVISVREEAD RPQPRLDRLT GKGMSTVVGR IREDSIFDIK FVVLSHNTIR GAAGGSIYNA
ELLVNEGLL
//
