ID A0A0W1ANJ1_9GAMM Unreviewed; 342 AA.
AC A0A0W1ANJ1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000313|EMBL:KTD82907.1};
GN Name=pdxB {ECO:0000313|EMBL:KTD82907.1};
GN ORFNames=Lwal_0385 {ECO:0000313|EMBL:KTD82907.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD82907.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD82907.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD82907.1,
RC ECO:0000313|Proteomes:UP000054729};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD82907.1}.
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DR EMBL; LNZB01000006; KTD82907.1; -; Genomic_DNA.
DR RefSeq; WP_058479237.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1ANJ1; -.
DR STRING; 66969.Lwal_0385; -.
DR PATRIC; fig|66969.6.peg.415; -.
DR OrthoDB; 9770208at2; -.
DR Proteomes; UP000054729; 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; 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; 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:UP000054729}.
FT DOMAIN 27..270
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..250
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 342 AA; 37829 MW; 8973D4016E0A0621 CRC64;
MKILADASLP GLETAFPAPF KLTKYAHQEE IPGMLSDQDI LLCRSTLKVD GELIRNHSLK
YVATASSGSD HIDHDYLVSK HIQAIDAKGC NAASVADYVM SCLAYLDKHK RALGKTAAVI
GLGMVGSQVF KRLKRLGFTV KCYDPPKSDR ESTFKTCSME EILDCDVICI HAELQKEGLN
PSFNLINAQI LDSLKPNCML INAARGGIVN EQDLIDCKLP LVYCTDVYSN EPNISKAIVE
RATLCTPHIA GHSLEAKYNA VTMVSHKLHT ILGLPIPKCS EPQKPHPINL NLDWQDLALS
IYNPINETDK LKSAEDLGKA FIELRSLHNV RHDFSNYGYL IL
//
