ID A0A0Q4Y256_9BURK Unreviewed; 478 AA.
AC A0A0Q4Y256;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KQP13612.1};
GN ORFNames=ASF43_17005 {ECO:0000313|EMBL:KQP13612.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP13612.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP13612.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP13612.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP13612.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP13612.1,
RC ECO:0000313|Proteomes:UP000051560};
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:KQP13612.1}.
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; LMMV01000023; KQP13612.1; -; Genomic_DNA.
DR RefSeq; WP_056186064.1; NZ_LMMV01000023.1.
DR AlphaFoldDB; A0A0Q4Y256; -.
DR STRING; 1736316.ASF43_17005; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000051560; 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:UP000051560}.
FT DOMAIN 34..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 478 AA; 50506 MW; 330922B9460580C1 CRC64;
MSTLLAALRE ALGSTHVLTG DDATGYLTDQ HRRLTGRALA VVRPADTAQV AQVVRLCRQH
RTPIVPQGGN TGLMGAATPD GSGRAVLLSL GRLQRIRAID RDNDTLTVEA GAVLANVQQA
AREAGRLFPL SLGSEGSCTI GGNLSTNAGG TQVLRYGNTR ELVLGLEVVT AEGAVWDGLR
GLRKDNTGYA LRDLYVGSEG TLGIITAATL KLYPLPQAQH TALLAFGCIR DAVAFLSSAR
AGFGASLTAF ELMSDTALGL IAQHVPAQPL PLPLDAPWYA LVELSDSEGE AHARERFEAV
VSQAFEDGLV TDAAIAESLP QSDALWRLRD EALGLAQQRD GRNIKHDVSV PISRIPDFLA
ATAAALQARF PGVRPVAFGH LGDGNLHYNV SHAPSATPAE LFAAEDAIHE LVHDSVHAHG
GSISAEHGVG QTKRDLLPRY KSAVELDLMR RLKAAFDPLG LLNPGKVLAP HTAEESTP
//
