ID A0A0Q7YYX7_9SPHN Unreviewed; 474 AA.
AC A0A0Q7YYX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KQZ62082.1};
GN ORFNames=ASD67_22435 {ECO:0000313|EMBL:KQZ62082.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ62082.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ62082.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ62082.1,
RC ECO:0000313|Proteomes:UP000051141};
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:KQZ62082.1}.
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DR EMBL; LMGF01000005; KQZ62082.1; -; Genomic_DNA.
DR RefSeq; WP_056352358.1; NZ_LMGF01000005.1.
DR AlphaFoldDB; A0A0Q7YYX7; -.
DR STRING; 1736474.ASD67_22435; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051141; 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}.
FT DOMAIN 40..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 474 AA; 49600 MW; 4D94DDCCBD74A5B2 CRC64;
MTRPPTPDLL AQLAALLGPK GFATDDDSLA PWLTDWRGKY HGRAAAMLSP ATTAEVAAVV
RLCAAQDVAI VPQGGNSGMV GGATPDASGA QLLLSTRRMN RVRTIDRAAG LAVAEAGVIL
ENFHNAVLAE GFRFPLTLGG KGSATIGGLV STNAGGTQVL RHGTMRALVA GVEAVLPDGQ
VFDGLAPLKK DNRGYDLRHL LCGAEGTLGI VTAATLRLVP AAQDRATAWI GLESPDKALL
LLRQLDAAIG APLEGFEIVP HGCLDAVLRH IPQTRHPLGG DCPWYALVEL AGDKADDLSA
RLETQLAIAL QAGLIDDVVI AKNDRESDDF WRLRDSISEA ERAEGPAIQH DVSVPVDLMP
RFIADNPARL AAAFPGARAL SFGHLGDGNV HHHVQPPAGV DGRAWIAAHG EDASRLVYSH
VIELGGSLSA EHGIGQMKRD LFAALDSPTR LAALRAIKAG LDPAGLFNPG KLIG
//
