ID B2GID1_KOCRD Unreviewed; 628 AA.
AC B2GID1;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative phenol 2-monooxygenase {ECO:0000313|EMBL:BAG30553.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:BAG30553.1};
GN OrderedLocusNames=KRH_22060 {ECO:0000313|EMBL:BAG30553.1};
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30553.1, ECO:0000313|Proteomes:UP000008838};
RN [1] {ECO:0000313|EMBL:BAG30553.1, ECO:0000313|Proteomes:UP000008838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC {ECO:0000313|Proteomes:UP000008838};
RX PubMed=18408034; DOI=10.1128/JB.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009152; BAG30553.1; -; Genomic_DNA.
DR RefSeq; WP_012399274.1; NC_010617.1.
DR AlphaFoldDB; B2GID1; -.
DR STRING; 378753.KRH_22060; -.
DR KEGG; krh:KRH_22060; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_9_2_11; -.
DR OrthoDB; 4246007at2; -.
DR Proteomes; UP000008838; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:BAG30553.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAG30553.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008838}.
FT DOMAIN 33..403
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 434..592
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 628 AA; 70155 MW; 659A4819BA9A8572 CRC64;
MLFHQNGYVS EDPRIEEARG HGIDRPEDLP DTMDVLIVGS GPAGVIAAAQ LSQYPEVSTR
LIERRPGRLE IGQADGIQAR SVETFQSFGF AQEIIQEAFM LREMCFWNPD PTNPQNIVRT
GRPADDPHGV SEFPHMIVNQ ARVMDYFLRS AKRGPGRIEP DYGIEFVGLE INQDHEHPVA
VTVRYAAGPR EGEERTVRAK YVFGCDGAAS RVRKSIGRKL EGQGANHAWG VMDVLANTDF
PDIRTKCAIN SVNGSILLIP REGGLLFRMY VDLGEVPEDD NHEIRKTPVE EVIRRANQII
HPYSVDVKSV AWSSVYEVGH RLTDHFDDVD TEDRGTRCPR VFIAGDACHT HSAKAGQGMN
VSMQDGWNLG WKLGAVLSGR ADASLLDTYS EERQVIAKNL IDFDREWSML MATPQDKLPD
PKYLEEFYVK TAEFPAGFMT EYRPSLIVAG TEHQDLAKGF PVGKRFKSAE VQRVCDAMVV
HQGHEATADG RWRIHVYADA AVAGADSPTT AFAQWLHNDP TSPLVAFRRE GDGEATLFDV
DVTYQQPYDQ VDINAVPRAF KPQVGPFELN YWERVYAVIP GNDIFEQRTI SRDGAVVVVR
PDHYVAAVLP LDATAELAEF FSGFLRRD
//
