ID I7JS47_9BURK Unreviewed; 474 AA.
AC I7JS47;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CCG20062.1};
GN ORFNames=KUM_1282 {ECO:0000313|EMBL:CCG20062.1};
OS Taylorella asinigenitalis 14/45.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Taylorella.
OX NCBI_TaxID=1091495 {ECO:0000313|EMBL:CCG20062.1};
RN [1] {ECO:0000313|EMBL:CCG20062.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=14/45 {ECO:0000313|EMBL:CCG20062.1};
RX PubMed=22541164; DOI=10.1016/j.vetmic.2012.03.041;
RA Hauser H., Richter D.C., van Tonder A., Clark L., Preston A.;
RT "Comparative genomic analyses of the Taylorellae.";
RL Vet. Microbiol. 159:195-203(2012).
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; HE681424; CCG20062.1; -; Genomic_DNA.
DR AlphaFoldDB; I7JS47; -.
DR KEGG; tat:KUM_1282; -.
DR HOGENOM; CLU_017779_4_1_4; -.
DR BioCyc; TASI1091495:G13GE-1275-MONOMER; -.
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 33..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 474 AA; 51798 MW; A04A0621BF4785D0 CRC64;
MSLLEDLVAL VGSEHVLTGE EASPYLTDWR NRYSGRCLAV VKPADTEELA EVVKLCQQAD
APMVPQGGNT GLCGGATPSK KGDAVIILLS RMNKVLDVDT ANDTMTVQAG CILQDVQDAA
DKAGRLFPLS LGAEGSCTIG GNLATNAGGT QVLRYGNARD LCLGLEVVTA EGDIVNTLKS
LRKDNTGYDL RNLFIGSEGT LGIITAATLK LFPKPAAVTT AFLALEGFEQ AIEVLNRSKR
QFDASLTGFE LISDYCLSIV QKHLSHIRIP FPVDTAPWYV LMEISDSEGE DHAREMFERV
IGEAFENNEI LDAVIAESIQ QSNELWHLRE AVPLAEAEVG KAIKNDISIP VSKMDEFVRI
TNAKLQEFMP GIQMSVFGHL GDGNLHYNVC PPDDERKADF LTHQDEIFKI VFDSVHEFDG
SISAEHGIGQ LKRDILPEYK DENAMWIMRK IKRALDPNSL LNPGKVISSV EINP
//
