ID J2ZQF7_9LACO Unreviewed; 315 AA.
AC J2ZQF7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glyoxylate reductase NADP(+) {ECO:0000313|EMBL:EJN55146.1};
GN ORFNames=A11Y_111564 {ECO:0000313|EMBL:EJN55146.1};
OS Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN55146.1, ECO:0000313|Proteomes:UP000007271};
RN [1] {ECO:0000313|EMBL:EJN55146.1, ECO:0000313|Proteomes:UP000007271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA Rodriguez J.M.;
RT "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:EJN55146.1}.
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DR EMBL; AKFP01000077; EJN55146.1; -; Genomic_DNA.
DR RefSeq; WP_003679948.1; NZ_AKFP01000077.1.
DR AlphaFoldDB; J2ZQF7; -.
DR STRING; 1185325.A11Y_111564; -.
DR PATRIC; fig|1185325.3.peg.2306; -.
DR Proteomes; UP000007271; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000007271}.
FT DOMAIN 34..100
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 101..276
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 34309 MW; 6DDB7F2669CA8A19 CRC64;
MNILTATHFS TAQISQLESL PDVHVIRQND FQPKLAPTID VIMAWSPLAA KILAGPNRVK
FIQTSSAGID YLPLAALDQQ KVLVAHAGGI HGDAIAQSVL GYILDFARYI THPQNRDPQN
FWQGRIQRRV LYSVVNKRVL IYGTGHVGQA VSQLLRQIGL QTIGVNHSGH PAPEFTETIA
LATSKAQPPV ADFIVNTLPL TNATQHFFAA DFFARQPQPP IFINVGRGPS VDTTALIAAL
KNGQLAGAAL DVFEQELLPT DSPLWQAPNL LMTPHTTGTV DHVEDALFAI FYPNLQSFCQ
TGKLSVNQAD LKLGY
//
