ID A0A0R2FMU0_9LACO Unreviewed; 400 AA.
AC A0A0R2FMU0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KRN25805.1};
GN ORFNames=FD14_GL000214 {ECO:0000313|EMBL:KRN25805.1};
OS Secundilactobacillus similis DSM 23365 = JCM 2765.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN25805.1, ECO:0000313|Proteomes:UP000051442};
RN [1] {ECO:0000313|EMBL:KRN25805.1, ECO:0000313|Proteomes:UP000051442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN25805.1,
RC ECO:0000313|Proteomes:UP000051442};
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 -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:KRN25805.1}.
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DR EMBL; AYZM01000061; KRN25805.1; -; Genomic_DNA.
DR RefSeq; WP_054736747.1; NZ_BBAD01000049.1.
DR AlphaFoldDB; A0A0R2FMU0; -.
DR STRING; 1423804.FD14_GL000214; -.
DR PATRIC; fig|1423804.4.peg.233; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000051442; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000051442}.
FT DOMAIN 28..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..262
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 400 AA; 44771 MW; 87DCC134AD9219CA CRC64;
MYQINALDQF DVTDYAGDVF QLKDTTTPDA VLVRSSQVPD DLISHRLLLV ARSGIGTNTI
NIPACTANGT AVFNTPGANA NAVKELVVQC LFRYVRPLYP AIKNTTTLTA DNLQDAAEAT
RKDYIGEELY GKTVGILGLG AIGQRLANTC YHIGMQVVGY NRSFKNLQHV QQLETVDEVL
EQSDFVIILL PLTDETKGML STDQFRLMKD TAILMNFGRG EIVDNQAVIN ALEEGQFSRY
ITDFPHNDFK DNPNVVMMPH LGGNTVEALS HSANLTLQNT LDFLESGTIR SSVNFPPADL
PFTSPHRVTF FFKARQDFWA DVAHILNKHE IPVRELMSNF RDDYGYTIVN IDLTEIHKEI
GELKEIHDQL MHLDGMIRIR LLKNPSERVE SAEMEHGTAL
//
