ID A0A0Q5YSY5_9BURK Unreviewed; 1868 AA.
AC A0A0Q5YSY5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN ORFNames=ASG30_15620 {ECO:0000313|EMBL:KQT08909.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT08909.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT08909.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT08909.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT08909.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT08909.1,
RC ECO:0000313|Proteomes:UP000051173};
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|RuleBase:RU003968}.
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:KQT08909.1}.
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DR EMBL; LMQL01000013; KQT08909.1; -; Genomic_DNA.
DR RefSeq; WP_055900862.1; NZ_LMQL01000013.1.
DR STRING; 1736365.ASG30_15620; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF09423; PhoD; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT DOMAIN 104..127
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1868 AA; 203432 MW; 3339E2AE6773DC70 CRC64;
MSTDPRWSEP VESLLEGPAP HACDVLVIGS GYGGSIAAAE LAAPGRSVWV MERGREYVLG
EFPEDIGQLP GHVRFQRQGE DNPIGNADAL LDFRLFDEVG VLLANGLGGG SLINAGVALR
PPADLFEQAC WPAAYRPGGA AHGALSEALG QAVQKLEAEP LPKARELPKV AALSRLGEAI
GCGPAEAVPL TIAHQPRTTA QGIAQEACIR CGNCFTGCNV GAKGTLLTNL IPAAAARGAR
FYTGATALEI EPLPGPQRRW RVHFGLTARA KAEPSQRHFS VDTHTLVLSA GTLGSTELLL
RSPRVGCSSW LGHSFSGNGD TLAMGWGQEQ PVNGVSAPRP TSTQPSRDVG PTIAGTLRTT
VWVDGRRRPV LVQDGAVPSA LSMAVLALGS TLSSLHRYTQ ENAPAFHGAA APDVLATPER
IGEHAMLLLA MGRDDAKGRM LLRPGKGSRP VLDIQWPKGP SGDAAVGGRA PYFEALHEML
GKAHGKNGFD GGDYLPNPMW RPVPDKFTGI TGGSQPERLV TVHPLGGCAM ADDAAAGVVD
RFGEVFSGRT GTAVHAGLHV LDGAIVPCAV GVNPFVTISA LCLLAAREIR TRLDTRTATP
APLPMLLRLP SGQPAADRRQ PFVGAGPVVL AFEERLQSAD PTEVPEWMRP LIADPQVYAP
DPAGQPRAWV VQVKVQLDVH RWLADPSIAL DATLSLYANP WPESPTVRAE VMRPDHLVLQ
GPGKVTLLAP DFPGRAGERW ARGAEAFRTY VARRSARDLQ GNFGAGPSWS EAKDLFQRAG
LNHADYRELR YEFELGSKKL AYKVRASGLK RLAYRRQERN LWDALTRLDL KLQPGNGGKP
WPLGFDVDLV DMVRNRRLQV VQAPNTPAAI LAVGGFVALW LRALLRTHFW SFRGMSYDKL
KPVKVPPPPK LVPGGAWPPV EPRIVPLRVD RGHGEGGPIE LQLVHYPALD KVLEPRRALL
FIHGLAHGSG VFTTDTIGSD NLATYFLRQG YDIWLLDHRL SNRLPYAGEA HTMDIVARND
IARAIAEVRS RAGVAQVDVF AHCVGAGAFA MAVLGEHVPA GTIGHVILHA VHPWVVPSMS
NRFSGALAAL YKDFLGGDEK IVPVPPAGRG RAMDELIDRF AASLPWPQAE REPHERHKYD
PRGGWGVCNR MTVFYGREWE HGNLAPQTHD RLAELVGEAG IEVFRQLFFV IQRERLTDRE
GVNAYLTRNR LLKSWTFPTL FAHGGRNKVF DPRSAVRSWQ RMGRIFENAR EGQRTVRLFV
QQGYGHMDFL FGRQAYRDIY PRLAQFLKDA PGFHSAVGGK PARKYEANRV DGEDIGDYEY
LAPVQPWCGP LLQLHGWNGR PRELVLWFEQ RGDTTGEPEP PGLRINGKEV VGDAQAVRPP
SQFPFGPKSG NPTVSQGLGY HWTVTVPDTG SRRFEAMDHL EVAMNTAGGG DKRIGANHLG
GPWIAPGTNS IKLPLKFLRS SGGAAPAPSA PAEPRKRPPF ESETVSVLSF SGLPWWNRWL
GRLAADVPVS LLASSCRWPG TPFERKAADA LATRMLEHVE DQTRPVDALV LLGDQIYADA
TANVAETTEK AERGQDRYRA AWEGEATGLL MRHLPTWLVV DDHEFGDNVD GAGGPDFANG
FEAAMAWQWR WRKGQQGPAL PAPGQAVRGF WYEFAIGGLP AFAADTRSER EPRSGVNWRQ
ARLMGRDQLE AIKDWLRRHR TTPKFLCSGS VLGLPERRVL ESPSLARHAD DWTGYPATWQ
ELARFIAAEG IRNLVFLSGD YHLSAVAELE IRAVGAAAPV RAVSVVASGW NATLPFANPR
VFDHAWEQKV RLPACCESVD VWASARCLSR AHRQFTKLSV VPADAGWALE VASYDEHGGV
TKVAPLRL
//
