ID F9N4H5_9FIRM Unreviewed; 318 AA.
AC F9N4H5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=S-adenosyl-L-homocysteine hydrolase, NAD binding-like domain protein {ECO:0000313|EMBL:EGS38393.1};
GN ORFNames=HMPREF9200_0942 {ECO:0000313|EMBL:EGS38393.1};
OS Veillonella sp. oral taxon 780 str. F0422.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=944564 {ECO:0000313|EMBL:EGS38393.1, ECO:0000313|Proteomes:UP000010295};
RN [1] {ECO:0000313|EMBL:EGS38393.1, ECO:0000313|Proteomes:UP000010295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0422 {ECO:0000313|EMBL:EGS38393.1,
RC ECO:0000313|Proteomes:UP000010295};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGS38393.1}.
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; AFUJ01000016; EGS38393.1; -; Genomic_DNA.
DR RefSeq; WP_009353153.1; NZ_AFUJ01000016.1.
DR AlphaFoldDB; F9N4H5; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000010295; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; cd12161; GDH_like_1; 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; 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 SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Hydrolase {ECO:0000313|EMBL:EGS38393.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000010295}.
FT DOMAIN 14..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 34277 MW; ED9B1A7D60AD1D64 CRC64;
MKQIVVMEPL GVSETLLQSL AEPFKAEGYE LVVYGTKETN QIKLLDRVRQ ASIIILANQP
LSGEIIRQCP KLEFISVAFT GVDHIDLEAC HEKGIIVSNA AGYSTQAVTE LVFGLAISVL
RNVLPCDGRT RTGGTKDGLP GFELYGKTFG IVGTGAIGSA VARIAKAFGC KVIAYNRSEK
PELVAEGITF TDLDTVVQEA DILSLHVPLT EETRHVIDAK RIDMMKDTAV LINTARGPVV
DNEALAKALH AGKLRGAGID VFEVEPPIPT DHPLCDAPRT VLTPHIAFAS QEAFVTRAHI
VMDNIVAFLK GEPVNRVC
//
