ID E1V493_HALED Unreviewed; 298 AA.
AC E1V493;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:CBV40930.1};
DE EC=1.1.1.60 {ECO:0000313|EMBL:CBV40930.1};
GN Name=glxR2 {ECO:0000313|EMBL:CBV40930.1};
GN OrderedLocusNames=HELO_1047 {ECO:0000313|EMBL:CBV40930.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV40930.1, ECO:0000313|Proteomes:UP000008707};
RN [1] {ECO:0000313|Proteomes:UP000008707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000313|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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DR EMBL; FN869568; CBV40930.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V493; -.
DR STRING; 768066.HELO_1047; -.
DR KEGG; hel:HELO_1047; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_0_6; -.
DR OrthoDB; 9786703at2; -.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBV40930.1}.
FT DOMAIN 6..163
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 168..287
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 174
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 298 AA; 31069 MW; BE7270695F86401D CRC64;
MHDIRTIGVL GTGIMGGPMA ARLARAGWPL KVWNRSREKA MALADAGDVT LVCEPHAAAT
DVDALIVMLS SGPVCNEILL GEHGALTAMR PGSLLLVMSS IPVGTARQQA GAARRHDIAY
LDAPVSGGER GAIEGNLAIM VGGGASAFAR AESLLGVLGS PVHVGPEGCG QLAKLANQLI
VANGIATVAE ALLLAERGGA DPARVCEALQ GGFADSTILR VHGQRMLEGY HEPGGPAKWQ
SKDTRTAMAF ADSLALELPV SRLVDRLFNE LVEHGDGNLD HSALIRELRR INRLPVEG
//
