ID A0A258TU74_9PROT Unreviewed; 155 AA.
AC A0A258TU74;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Aspartate/homoserine dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF03447};
GN ORFNames=B7Y41_05440 {ECO:0000313|EMBL:OYY94996.1};
OS Hydrogenophilales bacterium 28-61-23.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY94996.1, ECO:0000313|Proteomes:UP000215898};
RN [1] {ECO:0000313|EMBL:OYY94996.1, ECO:0000313|Proteomes:UP000215898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-61-23 {ECO:0000313|EMBL:OYY94996.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYY94996.1}.
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DR EMBL; NCGJ01000003; OYY94996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258TU74; -.
DR Proteomes; UP000215898; Unassembled WGS sequence.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF03447; NAD_binding_3; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
FT DOMAIN 36..119
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 155 AA; 16982 MW; 3582C0678DC9F4CB CRC64;
MRGLGLALNR PACSQPQSTT QEETRVSNKI KVALLGLGSV GEAFAEHFLA KIQEDRIDVE
IVAVADRHPD TPVALGFAHS KVPVFQDAME VIKLGDQVDL IFDLTGNAEL RQQLRAGLQA
SNNRHTVIAP EVFAHLLWNF FGESKALLQH AQTGY
//