ID A0A0W0U8Z2_9GAMM Unreviewed; 461 AA.
AC A0A0W0U8Z2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cytokinin oxidase {ECO:0000313|EMBL:KTD04368.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:SPX62836.1};
DE EC=1.5.99.12 {ECO:0000313|EMBL:KTD04368.1};
GN Name=dprE1_2 {ECO:0000313|EMBL:SPX62836.1};
GN ORFNames=Lfee_0195 {ECO:0000313|EMBL:KTD04368.1}, NCTC12022_03604
GN {ECO:0000313|EMBL:SPX62836.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTD04368.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTD04368.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTD04368.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPX62836.1, ECO:0000313|Proteomes:UP000251942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX62836.1,
RC ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; LNYB01000008; KTD04368.1; -; Genomic_DNA.
DR EMBL; UASS01000040; SPX62836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0U8Z2; -.
DR STRING; 453.Lfee_0195; -.
DR PATRIC; fig|453.4.peg.216; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR015345; Cytokinin_DH_FAD/cytokin-bd.
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; PTHR13878:SF102; CYTOKININ DEHYDROGENASE 5; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF09265; Cytokin-bind; 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 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KTD04368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698}.
FT DOMAIN 40..209
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 461 AA; 51631 MW; 973F3584D486C715 CRC64;
MQPMPWSMSQ IKQCEKESGQ AMLSDEHALA SYAQDFGKLN QVIPSAVCIP SSIKKLQSVL
AYANQHNLNV TIRGNGLSQG GQALAQQGSL IMHLEQLNHV QTHEQASIWV EANATWSSLV
EVSLKKAQIP YVLPYNCNLS IGGVLSAGGV GSSSFKFGSI SSHVKALEVT TADGKTSQVD
EQSELFHACL SGQGRFAVIT KACIKLRPCL KQVRTFFLVY LDKNQWLHDL ADIKSGADYV
EAFCSPSLQG AKLTAEGKRL PFAQWLFALH ISLEYDSKPP QLNAVSKHLK PWKTIHIQDE
SIHSYLHRHN SRFEVMKLTG QWDLLHPWYE CFIPTSVLSR DLEELLTQLP IHYATVLQIV
PLANERRIGF LMLPDSKDIC ALMILNPGVN PVLLPSCLQA MTILDEHFLQ QGGKRYLSGY
LGQKLAKNYW QTHFGPAYGD WLQLKKKYDP RHILTSSLHY L
//
