ID D4CUV2_9FUSO Unreviewed; 320 AA.
AC D4CUV2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFE86862.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFE86862.1};
GN Name=pdxB {ECO:0000313|EMBL:EFE86862.1};
GN ORFNames=FUSPEROL_01193 {ECO:0000313|EMBL:EFE86862.1};
OS Fusobacterium periodonticum ATCC 33693.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=546275 {ECO:0000313|EMBL:EFE86862.1, ECO:0000313|Proteomes:UP000003748};
RN [1] {ECO:0000313|EMBL:EFE86862.1, ECO:0000313|Proteomes:UP000003748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33693 {ECO:0000313|EMBL:EFE86862.1,
RC ECO:0000313|Proteomes:UP000003748};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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:EFE86862.1}.
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DR EMBL; ACJY01000061; EFE86862.1; -; Genomic_DNA.
DR RefSeq; WP_005972825.1; NZ_GG665896.1.
DR AlphaFoldDB; D4CUV2; -.
DR STRING; 546275.FUSPEROL_01193; -.
DR GeneID; 78419443; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_0; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000003748; Unassembled WGS sequence.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 22..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 36403 MW; 53DEB0B25CB19C43 CRC64;
MENKLKIIFL DRNTVGPFEL KEIFSKYGEY TECNLTNDDD VASYLKDYDV IILNRIRLGK
KEFEKAPNLK LVLLTGTGFN HIDLIAAKEH GVSIANVAGY STNSVSQLTM TFLLNELTKV
EKLSQKVKEN KWNELSINMD RYYHIDTEDK ILGILGYGNI GQKVAEYAKS FGMKVMVAKI
PGREYTDSSD NRYDLDEVLE KCDIFSIHAP LTDLTKNLIN LDKMKKMKKS AIILNLGRGP
IINEDDLYYA LKNNIIASAA TDVMTTEPPQ KDCKLLELDN FTVTPHLAWK SQKSLERLFA
EIENNLNLFL ENKLIGVESK
//
