ID G9EMK8_9GAMM Unreviewed; 357 AA.
AC G9EMK8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LDG_6476 {ECO:0000313|EMBL:EHL31544.1};
OS Legionella drancourtii LLAP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL31544.1, ECO:0000313|Proteomes:UP000002770};
RN [1] {ECO:0000313|EMBL:EHL31544.1, ECO:0000313|Proteomes:UP000002770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL31544.1,
RC ECO:0000313|Proteomes:UP000002770};
RX PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., Fournier P.E.,
RA Greub G.;
RT "Insight into cross-talk between intra-amoebal pathogens.";
RL BMC Genomics 12:542-542(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; JH413813; EHL31544.1; -; Genomic_DNA.
DR RefSeq; WP_006870406.1; NZ_JH413813.1.
DR AlphaFoldDB; G9EMK8; -.
DR STRING; 658187.LDG_6476; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_4_0_6; -.
DR InParanoid; G9EMK8; -.
DR OrthoDB; 9770208at2; -.
DR Proteomes; UP000002770; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12158; ErythrP_dh; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR020921; Erythronate-4-P_DHase.
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096};
KW Reference proteome {ECO:0000313|Proteomes:UP000002770}.
FT DOMAIN 29..269
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..251
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 357 AA; 39773 MW; 81F4B5F50059EB20 CRC64;
MNILADGSLP GLKQAFPEPF HLTLYHHLDD VAQLIPGQDI LLCRATLKVN HSLLKNHSLR
YVATATSGTD HLDYPWLTSQ NIQVIDAKGC NARAVADYVV SALAYVEQHH LIQGNKAGII
GFGKVGSQVA ARLQAAGFEL LTYDPLKELR EPNTFQSCQF DDLSQADLLC IHAELHDTQP
HPSLNLINQP FLEHLKSGCV IINAARGGII NEEALLNNHK TLSYCTDVYL NEPAVDQRII
ERTTLCTPHI AGHSLEAKYL AVAMVSERLH QIIGLPSPQF AIPELKHIFA LKNDKTWEEN
VLSIYNPLDE TILLKEATDK ESAFLTLRKN HHQRHNFQLY ANSALDKKSR LLLGETG
//
