ID A0A0N0KCT9_9SPHN Unreviewed; 342 AA.
AC A0A0N0KCT9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KPF89106.1};
GN ORFNames=IP83_03800 {ECO:0000313|EMBL:KPF89106.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF89106.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF89106.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF89106.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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:KPF89106.1}.
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DR EMBL; LJHZ01000018; KPF89106.1; -; Genomic_DNA.
DR RefSeq; WP_054120885.1; NZ_LJHZ01000018.1.
DR AlphaFoldDB; A0A0N0KCT9; -.
DR STRING; 1523427.IP83_03800; -.
DR PATRIC; fig|1523427.4.peg.1358; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000037906; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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: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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 22..337
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 127..306
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 342 AA; 37408 MW; B943EFAF16FD6306 CRC64;
MPANPPSTDY RTTRRIEGRP RVFVTRRLLP ETEARMAELF DVTLNPDDRP LSQDEIRAAM
QEAHVLVPTV TDRIDAELIA AAGPQLGLIA SFGAGTDHID LAAARARKIL VTNTPGVFTD
DTADMTMSLI IAVSRRLAEG GRVIRSGDWA GWAPSTLLGH RISGKRLGII GMGRIGQAVA
HRARAFGLEI VYHNRQRLPE AFERMVGARY EADIDTLVRE SDIVTLHCPS TPETHFIMDA
RRIALMKPEA YLVNTARGDV VDENALIEAL QEGRIGGAGL DVFAHEPKID PRLLALGNVS
LLPHMGSATF EGRTASGDKV IANIRFWADG HRPPDQVLEG WA
//
