ID L1KW18_9ACTN Unreviewed; 337 AA.
AC L1KW18;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EKX64739.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EKX64739.1};
GN Name=pdxB_5 {ECO:0000313|EMBL:EKX64739.1};
GN ORFNames=STRIP9103_07906 {ECO:0000313|EMBL:EKX64739.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX64739.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX64739.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX64739.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-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:EKX64739.1}.
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DR EMBL; AEJC01000353; EKX64739.1; -; Genomic_DNA.
DR AlphaFoldDB; L1KW18; -.
DR PATRIC; fig|698759.3.peg.4617; -.
DR Proteomes; UP000010411; 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 CDD; cd12167; 2-Hacid_dh_8; 1.
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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000010411}.
FT DOMAIN 39..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 122..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 337 AA; 35857 MW; 94F6624C1C4BC076 CRC64;
MPSAQSPRAV FAMDPVHLPL LFPPPLMARL RQVVEIDPEL VVQDFADPAA APALAGAEVL
ITGWGCPHLD ADVLAAAPGL RHVLHAAGSV RALVGEALWQ RGVTVSSAVV GNALPVAEYT
LAMILLAGKD AFDQRERFRQ THAYPSPAET ATIGNVGRRV GVIGASRVGR RLLELLRPFD
FAVSLYDPYV APAGAAALGA EPKGLDDLLR TSDIVSLHAP DIPETYRMLD RGRLALIRDG
GVLINTSRGA LIDPDALTEE LLSGRLKAVL DVTEPEPLPA ASPLYNLPNV FLTPHIAGSL
GNELERLGRT VVEELERVAA GQPPAHEVRH TDLARVA
//
