ID A0A0Q4KV77_9SPHN Unreviewed; 311 AA.
AC A0A0Q4KV77;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KQN26007.1};
GN ORFNames=ASE86_07500 {ECO:0000313|EMBL:KQN26007.1};
OS Sphingomonas sp. Leaf33.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN26007.1, ECO:0000313|Proteomes:UP000051455};
RN [1] {ECO:0000313|EMBL:KQN26007.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26007.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN26007.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26007.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN26007.1}.
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DR EMBL; LMLB01000001; KQN26007.1; -; Genomic_DNA.
DR RefSeq; WP_056424150.1; NZ_LMLB01000001.1.
DR AlphaFoldDB; A0A0Q4KV77; -.
DR STRING; 1736215.ASE86_07500; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000051455; 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 CDD; cd05300; 2-Hacid_dh_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; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000051455}.
FT DOMAIN 26..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 104..272
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 311 AA; 33226 MW; 8C44CBCD23099983 CRC64;
MKAVLPALAR PLLEPHLPAG LDIAWFASAQ QAREMIADAD IAWVDMQPPS ETAAAIAAGQ
RLKWVSTIYA GVDAFDLPRL KALGAVLTNG AGINAVAVAE YAVMGMLVAA KRYDQVVRQA
DRQEWTIAAP GTVELEDTSA LIIGYGTIGR LIGDRLRAFG VQVTGVTRTG RDDTLTPDQW
RGRIGAFDWI VLAAPATTDT HALIGADEIA AMKPGAWLIN MARGDMVDQD ALIAALSARR
IAGAFLDTVT PEPLPAGHPL WTTPNAIHSM HLSGRSQTQM FQRGAALFLR NLSAFLSGNP
LQNRVDLDAG Y
//
