ID   FAS5_RHOFA              Reviewed;         438 AA.
AC   P46377;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Uncharacterized oxidoreductase ORF5 in fasciation locus;
GN   Name=fas5;
OS   Rhodococcus fascians.
OG   Plasmid pFiD188.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=8169198; DOI=10.1128/jb.176.9.2492-2501.1994;
RA   Crespi M., Vereecke D., Temmerman W., van Montagu M., Desomer J.;
RT   "The fas operon of Rhodococcus fascians encodes new genes required for
RT   efficient fasciation of host plants.";
RL   J. Bacteriol. 176:2492-2501(1994).
CC   -!- FUNCTION: The FAS-operon encodes genes involved in cytokinin production
CC       and in host plant fasciation (leafy gall).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- INDUCTION: During the interaction with host plants.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; Z29635; CAA82745.1; -; Genomic_DNA.
DR   PIR; E55578; E55578.
DR   RefSeq; YP_007878708.1; NC_021080.1.
DR   AlphaFoldDB; P46377; -.
DR   SMR; P46377; -.
DR   STRING; 1443905.GCA_000761075_00036; -.
DR   GO; GO:0019139; F:cytokinin dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.10; -; 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   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Pfam; PF09265; Cytokin-bind; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase; Plasmid.
FT   CHAIN           1..438
FT                   /note="Uncharacterized oxidoreductase ORF5 in fasciation
FT                   locus"
FT                   /id="PRO_0000128172"
FT   DOMAIN          23..193
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   BINDING         55..59
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         430..433
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         60
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   438 AA;  47890 MW;  5F7FADA0911A0171 CRC64;
     MSGIWHTDDV HLTSAGADFG NCIHAKPPVV VVPRTVADVQ EALRYTAARN LSLAVRGSGH
     STYGQCQADG GVVLDMKRFN TVHDVRSGQA TIDAGVRWSD VVAATLSRQQ TPPVLTDYLG
     TTVGGTLSVG GFGGSSHGFG LQTDNVDSLA VVTGSGDFRE CSAVSNSELF DAVRGGLGQF
     GVIVNATIRL TAAHESVRQY KLQYSNLGVF LGDQLRAMSN RLFDHVQGRI RVDADGHLRY
     RLDLAKYFTP PRRPDDDALL SSLQYDSCAE YNSDVDYGDF INRMADQELD LRHTGEWFYP
     HPWASLLIPA DKIEQFIETT SSSLTDDLGN SGLIMVYPIP TTPITAPFIP IPHCDTFFML
     AVLRTASPGA EARMIASNRL LYEQARDVGG VAYAVNAVPM SPGDWCTHFG SRWQAIARAK
     RRFDPYRILA PGYRMSFD