ID C9M597_9BACT Unreviewed; 330 AA.
AC C9M597;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EEX49265.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EEX49265.1};
GN Name=pdxB {ECO:0000313|EMBL:EEX49265.1};
GN ORFNames=GCWU000246_00353 {ECO:0000313|EMBL:EEX49265.1};
OS Jonquetella anthropi E3_33 E1.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Jonquetella.
OX NCBI_TaxID=645512 {ECO:0000313|EMBL:EEX49265.1, ECO:0000313|Proteomes:UP000003290};
RN [1] {ECO:0000313|EMBL:EEX49265.1, ECO:0000313|Proteomes:UP000003290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3_33 E1 {ECO:0000313|EMBL:EEX49265.1,
RC ECO:0000313|Proteomes:UP000003290};
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., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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:EEX49265.1}.
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DR EMBL; ACOO02000004; EEX49265.1; -; Genomic_DNA.
DR RefSeq; WP_008520048.1; NZ_GG697147.2.
DR AlphaFoldDB; C9M597; -.
DR PATRIC; fig|645512.3.peg.1466; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_0; -.
DR Proteomes; UP000003290; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:EEX49265.1}.
FT DOMAIN 16..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 34726 MW; 09C5F847DB9C86F1 CRC64;
MGQKPLVTVI EPEGPMEWFS ELDGLGDVRF FTPSGPVSRE LTARLIGPSR AVIITSATAI
DAELIDKAKN LGIIAKCGGP PSNVDIPAAT RRGVAVSCVP GANTTTVAEY AAFLLLGLFR
RADSLACALK SGAWRGPDLL GRDMKGALIG VVGYGAIGRE VLARLLPFGP QVLVWSPSAQ
AAGVILPEGA RYARSLAELV SRCDAVSVHS RVTPETRNMF NREVFALFKP GAVFVNTARG
DLVDEDALAW ALTDGPLAAA AVDVFRQEPP DAASPLLSCP NLWATPHAAA WTRQALEREC
RGAAASVAAF LTGEPIPGLL NSPYQSFANK
//