ID A0A1P8WSD4_9PLAN Unreviewed; 341 AA.
AC A0A1P8WSD4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:APZ96977.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:APZ96977.1};
GN Name=ghrB {ECO:0000313|EMBL:APZ96977.1};
GN ORFNames=Fuma_06653 {ECO:0000313|EMBL:APZ96977.1};
OS Fuerstiella marisgermanici.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Fuerstiella.
OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ96977.1, ECO:0000313|Proteomes:UP000187735};
RN [1] {ECO:0000313|EMBL:APZ96977.1, ECO:0000313|Proteomes:UP000187735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH11 {ECO:0000313|EMBL:APZ96977.1,
RC ECO:0000313|Proteomes:UP000187735};
RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT Phylum Planctomycetes from the German Wadden Sea.";
RL Front. Microbiol. 7:2079-2079(2016).
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; CP017641; APZ96977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8WSD4; -.
DR STRING; 1891926.Fuma_06653; -.
DR KEGG; fmr:Fuma_06653; -.
DR Proteomes; UP000187735; Chromosome.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:APZ96977.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187735}.
FT DOMAIN 24..339
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 129..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 341 AA; 36661 MW; 26CE2929D31F014A CRC64;
MTASSRQFAP HFTDQEDMHN RPKVFVTRNI PSAGLAKIQA ATTCEVWPER MPPSPDVLAE
KASGCDGVLT LLSDRIDADF FDAVGSQLKV VSNFAVGYNN IDVAEATKRG IVVGNTPDVL
TDATADIAVA LMLAAGRCLR EGLENVVRKE WQTWEPMEFI GQDLSGKTLG IVGMGRIGHA
TAKRCHFGWG MNVIYTSRSD KPESDSELGA SRVTFEQLLA DSDFISVHTD LNPETSKMFD
SAAFSGMKSN AVFVNTARGG VVDQDALQKA LTNGEIFAAG LDVTEPEPLP DDSPLRDLPN
CFILPHIGSG TVKSRDAMAE IAADNLLAGL EGKPLRHQVT A
//
