ID A0A0T2QIK3_9SPHN Unreviewed; 477 AA.
AC A0A0T2QIK3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KRA84583.1};
GN ORFNames=ASD76_03050 {ECO:0000313|EMBL:KRA84583.1};
OS Altererythrobacter sp. Root672.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA84583.1, ECO:0000313|Proteomes:UP000051125};
RN [1] {ECO:0000313|EMBL:KRA84583.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA84583.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA84583.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA84583.1,
RC ECO:0000313|Proteomes:UP000051125};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:KRA84583.1}.
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DR EMBL; LMHH01000001; KRA84583.1; -; Genomic_DNA.
DR RefSeq; WP_055922868.1; NZ_LMHH01000001.1.
DR AlphaFoldDB; A0A0T2QIK3; -.
DR STRING; 1736584.ASD76_03050; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051125; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000051125}.
FT DOMAIN 38..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 477 AA; 50098 MW; ECBB49D094391FDB CRC64;
MTDQEQFLAA AGELLGERGL TRDPELLQPW LTDWRGRFSG RAMALASPAS TAEVSALMKL
CAEFGVPVVP QGGNSGMSGG ATPDETGHAM LLSLRRMNAI RHFDPTAREI TCEAGVILQT
LHEAAAAEHL RFPLTLGGKG SATVGGLIST NAGGTQVLRH GSMRTQVLGI EAVLADGKVF
DALVPLKKDN RGFDLKQLLI GSEGTLGIVT AATLRLLPAL ADRAVLWAGL ESVTAARALL
LHSETIAGDA LEGFEIMPRH SLEAVLAHVP GSRSPLQGQH EWNVLIELAA DAAGADALPA
LAQTLLETAF EAGLVEDATI AANEAQAEQF WLLRDEIAPA ERALGPAVQH DISVPVARMA
DFVSAAVPDV EARFPSTRAV AFGHLGDGNV HFHVLAPAGA VRGEWEAGDG KAISAFVHDL
VTQWGGSISA EHGIGQLKRD ELGRLGDPVQ LAMMRAVKHA LDPANLLNPG KLVPPCT
//
