ID A0A0Q6XBC2_9BURK Unreviewed; 468 AA.
AC A0A0Q6XBC2;
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:KQW00387.1};
GN ORFNames=ASC87_17680 {ECO:0000313|EMBL:KQW00387.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQW00387.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQW00387.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW00387.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW00387.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW00387.1,
RC ECO:0000313|Proteomes:UP000051465};
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:KQW00387.1}.
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DR EMBL; LMDI01000008; KQW00387.1; -; Genomic_DNA.
DR RefSeq; WP_056659016.1; NZ_LMDI01000008.1.
DR AlphaFoldDB; A0A0Q6XBC2; -.
DR STRING; 1736433.ASC87_17680; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000051465; 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:UP000051465}.
FT DOMAIN 35..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 49090 MW; B9A2A65EAEF73C3A CRC64;
MTTLLLEALT AAVGATHVLT DGDLAGWEQD WRKRYRGKAL AVVRPGNTAE VAAVVRACAA
HGASLVPQGG NTGLVGGSVP DSSGTQVLLS LSRLNRMRGL DAANLTLTVE AGCILQTVQE
TAEAAGLLFP LSLAAEGSCT IGGNLASNAG GTQVLRYGNA RELCLGLEVV TAQGEVWDGL
AGLRKDNTGY DLRDLYIGSE GTLGIITAAT LKLYPAPAAV MTALATVPSM DQAVALLQLA
QARLGPGLTG FEVMNGFSLG LVRKHFPQLR QPLPPSDWTV LLEQSDTEGE AHARALFEGL
LEAALEAGTI TDAAVAESLD QSHTMWHLRE SIPLAQAEEG LNIKHDISLP VSSIPAFVAE
TDALLSARWP GLRLVNFGHL GDGNLHYNVQ APEGQEAAEF LRDHEHAVNA VVYDAVGAHG
GSFSAEHGIG ALKRDDLAQR KSPVALQLMR AVKQALDPAG LMNPGRML
//
