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Database: UniProt
Entry: Q82XY9_NITEU
LinkDB: Q82XY9_NITEU
Original site: Q82XY9_NITEU 
ID   Q82XY9_NITEU            Unreviewed;       322 AA.
AC   Q82XY9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:CAD84012.1};
DE            EC=1.1.1.29 {ECO:0000313|EMBL:CAD84012.1};
GN   Name=hprA {ECO:0000313|EMBL:CAD84012.1};
GN   OrderedLocusNames=NE0101 {ECO:0000313|EMBL:CAD84012.1};
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD84012.1, ECO:0000313|Proteomes:UP000001416};
RN   [1] {ECO:0000313|EMBL:CAD84012.1, ECO:0000313|Proteomes:UP000001416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC   {ECO:0000313|Proteomes:UP000001416};
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA   Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA   Whittaker M., Arp D.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AL954747; CAD84012.1; -; Genomic_DNA.
DR   RefSeq; WP_011110753.1; NC_004757.1.
DR   AlphaFoldDB; Q82XY9; -.
DR   STRING; 228410.NE0101; -.
DR   KEGG; neu:NE0101; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_4; -.
DR   OMA; PHIAWAY; -.
DR   OrthoDB; 9805416at2; -.
DR   PhylomeDB; Q82XY9; -.
DR   Proteomes; UP000001416; Chromosome.
DR   GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12162; 2-Hacid_dh_4; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   PANTHER; PTHR43761:SF1; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001416}.
FT   DOMAIN          27..314
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   322 AA;  35783 MW;  6F719931C91FDB13 CRC64;
     MLTVFLDFGS VTRGDIDRTV LEQVVSPWVY HDNTSREQVA ERIREAEIVV SNKTLLDRSA
     LDAANKLKLI CVAATGYNNV DLIAAAERNI PVCNVRNYAT GSVAQHVFMF MLNFACRFVE
     YQQLIKRGGW QASSYFCPLD FGITELAGKT LGIVGYGELG NAVANIAKAF GMKLLIAEHK
     SASTIRPGRT AFDEVIRQTD FITLHCPLSE DTRHLISNRE LNLMKPSAYL INTARSGLID
     ETDLLKSLYS KHIAGAAIDV LKEEPPVSGN PLLDYPHPNL IITPHSAWAS VESRQRMLNL
     LADNIRNFLH NKPFNQIKDA LA
//
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