ID A3I1F8_9BACT Unreviewed; 332 AA.
AC A3I1F8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:EAZ79624.1};
GN ORFNames=ALPR1_08368 {ECO:0000313|EMBL:EAZ79624.1};
OS Algoriphagus machipongonensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ79624.1, ECO:0000313|Proteomes:UP000003919};
RN [1] {ECO:0000313|EMBL:EAZ79624.1, ECO:0000313|Proteomes:UP000003919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR1 {ECO:0000313|EMBL:EAZ79624.1,
RC ECO:0000313|Proteomes:UP000003919};
RX PubMed=21183675; DOI=10.1128/JB.01421-10;
RA Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., Imamovic A.,
RA Fairclough S.R., King N.;
RT "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a
RT colony-forming choanoflagellate.";
RL J. Bacteriol. 193:1485-1486(2011).
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:EAZ79624.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAXU02000001; EAZ79624.1; -; Genomic_DNA.
DR RefSeq; WP_008199793.1; NZ_CM001023.1.
DR AlphaFoldDB; A3I1F8; -.
DR STRING; 388413.ALPR1_08368; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_10; -.
DR OrthoDB; 1522997at2; -.
DR Proteomes; UP000003919; Chromosome.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003919}.
FT DOMAIN 8..328
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 332 AA; 36880 MW; 20BD9A7D46082AA0 CRC64;
MNVACFSTKS YDRESFDQLI PKHAHQFTYL EPKLDKHTVS LAEGYDAICA FVNDHLDAPV
LKKLAALNVK KIVLRCAGYN QVDLEKAAEY GIQICRVPAY SPEAVAEHAF ALILSLSRKT
HKAFNRVRDN NFSLEGLAGF NLHGKTIGVI GTGAIGKAFC SIALGFGCKV LAYDLIESKE
LKTMGVEYLG LDDLLMQSQV ISLHCPLTPG TKHLINKKTL ELMPKGVMII NTSRGALIET
KSVIRALKTK KIGYLGIDVY EQEEDLFFRD LSEEILMDEQ ITRLMSFPNV LITGHQAFLT
KEALNQIAAT TLFNLDEMEA GKKLTHEVKI ES
//
