ID A0A0Q4G055_9SPHN Unreviewed; 464 AA.
AC A0A0Q4G055;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ASE75_02940 {ECO:0000313|EMBL:KQM67858.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM67858.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM67858.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67858.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM67858.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67858.1,
RC ECO:0000313|Proteomes:UP000051777};
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:KQM67858.1}.
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DR EMBL; LMKL01000001; KQM67858.1; -; Genomic_DNA.
DR RefSeq; WP_055928446.1; NZ_LMKL01000001.1.
DR AlphaFoldDB; A0A0Q4G055; -.
DR STRING; 1735683.ASE75_02940; -.
DR OrthoDB; 9809290at2; -.
DR Proteomes; UP000051777; 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 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:UP000051777}.
FT DOMAIN 33..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 48329 MW; 8A692CB651667535 CRC64;
MTIASGLAAI VGLAHVLTGR EDDSRYHEDG RTGGGRALCV VRPGDVDQLA EVLRFAAAAD
LRVIAQGGRS GLVGAGLGSD ERDVIVSLER LVQPPSIDGA NRTAHVTAGV PLSMLNRAAA
EHGLTFPIDL GADPSIGGMI ATNTGGARLL RYGDVRRNVL SVDVMAADGT VSTFGRAVWK
DNSGLDLKQL VIGAGGATGL VTAATLALQP VPRATITAML ALDAMQGAVE LLREVEQAFG
TLLTAFEGIS AAALAAAITH VPRLTDPFPG RTPGYVVLIE LSAGAAFDAS DLEDRLGRVL
EPVMDMLVRD AVVDRGLRLW AIRHAIPEGL RGAGRVIACD IAVPRGAVPA FRARIVERIA
RISPMLVLHD FGHIGDGGVH ANMVWPTDAG PLDDAIVHAA RSAVLDIAVE EFGGSFSAEH
GVGPANLAAY VRHVPTRQRA LAGAVQRLMS PRPIGRIDFG EETA
//
