ID A0A0R2CTC3_9LACO Unreviewed; 292 AA.
AC A0A0R2CTC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:KRM94602.1};
GN ORFNames=FC56_GL001561 {ECO:0000313|EMBL:KRM94602.1};
OS Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM94602.1, ECO:0000313|Proteomes:UP000051256};
RN [1] {ECO:0000313|EMBL:KRM94602.1, ECO:0000313|Proteomes:UP000051256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM94602.1,
RC ECO:0000313|Proteomes:UP000051256};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM94602.1}.
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DR EMBL; AYZR01000004; KRM94602.1; -; Genomic_DNA.
DR RefSeq; WP_056977889.1; NZ_AYZR01000004.1.
DR AlphaFoldDB; A0A0R2CTC3; -.
DR STRING; 1423802.FC56_GL001561; -.
DR PATRIC; fig|1423802.4.peg.1582; -.
DR Proteomes; UP000051256; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000051256}.
FT DOMAIN 2..161
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 164..274
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 292 AA; 31228 MW; 595EBC73699C220A CRC64;
MKIGFIGTGV MGSAMIKNLL KADFAVTVYN RTKEHAQAVI AAGATWANSP AEVASQSDVV
ITMVGFPKDV KGVYFGSKGI FKRVHAGQVL VDMTTSSPKL AQQIFVEGKK RGVEVLDAPV
SGGDVGAQNA TLTVMVGGLE STYQKMQPVF SVVGQSITYF GAAGSGQNAK MANQIMIAGT
MTGMSEMLVY AKAANLDLEQ VIKTVDNGGG QNWSLANYGP RVLKGDYRPG FYAKHFLKDL
KIALDVADEM ELNLPATELA KRLYDRMVNG AGLGNESTDG LVNIYHSWRE DD
//
