ID A0A126ZA78_9BURK Unreviewed; 478 AA.
AC A0A126ZA78;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:AMM23504.1};
GN ORFNames=AX767_03400 {ECO:0000313|EMBL:AMM23504.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM23504.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM23504.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM23504.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-2016) 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}.
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DR EMBL; CP014517; AMM23504.1; -; Genomic_DNA.
DR RefSeq; WP_068628637.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZA78; -.
DR STRING; 1795631.AX767_03400; -.
DR KEGG; vaa:AX767_03400; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000070169; Chromosome.
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:UP000070169}.
FT DOMAIN 35..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 478 AA; 50728 MW; 62F5394A639CE7B4 CRC64;
MTALLLDELR AIVGAPNVLT EGDLTAWEQD WRKRERGKAL AIVRPANTAQ VAAVVKACAA
AGTAIVPQGG NTGLAVGSTP DDSGTQVLLS LQRMNAIRAI DPANLTVTVE AGCILQTLQE
AAEKAGFLFP LSLAAEGSCT IGGNLATNAG GTQVVRYGNT RDLCLGLEVV TPQGEVWDGT
SGLRKDNTGY DLRDLMVGSE GTLGIITAAT MKLYPQPAAR LTAWAAVPSL EHAVTLLGLA
HKHLGSGLTG FEVMGKFALS LVDKHMPQLR VPFIDDDAAP WCVLLENSDS ESEQHARARF
EALLETAFED GCVTDAVVAE NLTQAHQLWH IRENIPLAQA EEGLNIKHDI SIAVSRIPAF
VASTDALLQR EIPGVRLVNF GHLGDGNLHY NVQAPVDGDA KAFLDDEEAR VNTLVYDAVA
EFGGSFSAEH GIGGLKVDKL EKHKSPVALG MMRAIKRGLD PQNILNPGRV LRSQGPSS
//
