ID A0A0N0XH02_9NEIS Unreviewed; 324 AA.
AC A0A0N0XH02;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:KPC49071.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:KPC49071.1};
GN Name=ghrB {ECO:0000313|EMBL:KPC49071.1};
GN ORFNames=WG78_21165 {ECO:0000313|EMBL:KPC49071.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC49071.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC49071.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC49071.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:KPC49071.1}.
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DR EMBL; LAQT01000038; KPC49071.1; -; Genomic_DNA.
DR RefSeq; WP_053939981.1; NZ_LAQT01000038.1.
DR AlphaFoldDB; A0A0N0XH02; -.
DR STRING; 857265.WG78_21165; -.
DR PATRIC; fig|857265.3.peg.4332; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000037939; Unassembled WGS sequence.
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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:KPC49071.1}; Pyruvate {ECO:0000313|EMBL:KPC49071.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037939}.
FT DOMAIN 5..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 34996 MW; 1F96290CC43A67C2 CRC64;
MTQRVVVYKN LPEDLLAQLK ARFEITEVDS VDSDGPFAAA MAQADGVIGG GLSLPSAVLD
RASKLRTVAT VSAGFDQFDV ADLTRRGILL SNTPAALTET VADTVLMLML MTARRGAELA
EYVKAGQWQG SVGPDCYSSD VHGKTLGIVG MGRIGLAVGR RAKHGFGMNV RYHNRSQHPA
AEEALQAKWL PLDDLLRECD FVCVLLPLSA ETEKRFSMRE FALMQKHAFF INAGRGRVVD
EAALIAALQN GQIAGAGLDV FENEPLDVAS PLLKLPQVVA LPHVGSATHQ TRYDMAASAV
SNLIDALEGR LPEFMVNPQA WKRE
//
