ID Q2CH01_OCEGH Unreviewed; 308 AA.
AC Q2CH01;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:EAR52010.1};
GN ORFNames=OG2516_13334 {ECO:0000313|EMBL:EAR52010.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR52010.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR52010.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAR52010.1}.
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; AAOT01000007; EAR52010.1; -; Genomic_DNA.
DR RefSeq; WP_007256124.1; NZ_CH724108.1.
DR AlphaFoldDB; Q2CH01; -.
DR STRING; 314256.OG2516_13334; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_5; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000003635; 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:UniProt.
DR CDD; cd12164; GDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003635}.
FT DOMAIN 119..273
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 308 AA; 32822 MW; 1087B40776B06A57 CRC64;
MAGVLFLAGH RWPDYREVLP RAVAEAGVRA EVSPDLPAEA VDYIVYGPAR GAADFSRYPR
LKAVFSLWAG VESIVANPTL RVPLTRMVDP GLEAGMVEYV AGHVLRHHLG MDAHIHNPDH
AWAPRMPPLA SERTVAVLGL GALGAAAART LAGLGFAVRG WSRTAREVPG VTCHHGADGL
AAALAGAEML VLLLPLTEAT ERIVDAAALA RLAPGAVLLN PGRGALVDDA ALLEALDSGR
LGHATLDTFR TEPLPRDHPF WRHERVTVTP HIASETRPAT AARVIAENLR RAEAGEPLLH
LVDRGRGY
//
