ID A0A0P7ZTW7_9CYAN Unreviewed; 336 AA.
AC A0A0P7ZTW7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:KPQ33717.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:KPQ33717.1};
GN Name=ldhA {ECO:0000313|EMBL:KPQ33717.1};
GN ORFNames=HLUCCA11_17745 {ECO:0000313|EMBL:KPQ33717.1};
OS Phormidesmis priestleyi Ana.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ33717.1, ECO:0000313|Proteomes:UP000050465};
RN [1] {ECO:0000313|EMBL:KPQ33717.1, ECO:0000313|Proteomes:UP000050465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ana {ECO:0000313|EMBL:KPQ33717.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ33717.1}.
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DR EMBL; LJZR01000028; KPQ33717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZTW7; -.
DR STRING; 1666911.HLUCCA11_17745; -.
DR PATRIC; fig|1666911.3.peg.1350; -.
DR Proteomes; UP000050465; Unassembled WGS sequence.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12183; LDH_like_2; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
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}.
FT DOMAIN 3..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 336 AA; 36925 MW; 0A95715B94D5C8A5 CRC64;
MKVAVFSAKP YDRKFLTAAN IDHAHELVFL EARLTPETAA LAGGFPAVCA FINDQLNQQT
LGAIAASGTE LIALRAAGFN NVDLQAASEL NLTIVRVPEY SPYAVAEHAV GLILMLNRKL
NKAYNRVRDD NFALDGLLGF DLHGSTVGVI GTGKIGQIFC QIMTGFGCHV LAYDPYPNPA
CLEMGVEYRT LPDLLATADI ISLHCPLMPE TYHLLDQQSL SHLKPGAMVI NTSRGGLIDT
KAVIKAIKTG QIGYLGIDVY EQEENLFFED WSNTVVQDDD IQRLQSFNNV VITAHQAFFT
REALTNIAKT TMISLTQFER GEACEYQIHQ RQFGKA
//
