ID A0A077M5Y4_9MICO Unreviewed; 333 AA.
AC A0A077M5Y4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:CCI51949.1};
GN ORFNames=BN13_1330014 {ECO:0000313|EMBL:CCI51949.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI51949.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI51949.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI51949.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:CCI51949.1}.
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DR EMBL; CAJC01000039; CCI51949.1; -; Genomic_DNA.
DR RefSeq; WP_048548198.1; NZ_HF571038.1.
DR AlphaFoldDB; A0A077M5Y4; -.
DR STRING; 1193518.BN13_1330014; -.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000035720; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; 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 SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:UP000035720}.
FT DOMAIN 129..293
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
SQ SEQUENCE 333 AA; 35214 MW; 8AE8CBFB287C795B CRC64;
MAKVVVISRA GCASLPAHAI ERLRRRHTVE FVQRQTAPNR TTAVELLRGA TVLAATNVTL
PRLTPDLLDD LPDLRHVVLY ATGYEHIDVT ALADRGVTLS TLPEYATNAV AEHALGLIFA
SATRIHLAND RARGRVAADV SLRGVEITCR TLAVIGLGRI GTRLAALAGA LGMRVLGVDI
DPAARARAAT GGMPVLGLHD ALAAADFVAV TASTVPGTVP ILGGSELALL HRDAFVVNVG
RPVLVDQEAM RAALLREDLR GYAVDEVCFD PGHPADRLLL DEGRVLQSAH SAWWRDEVLA
RGAEMFASSI AAAADGCPVH VVSARPKLLP LAR
//
