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Database: UniProt
Entry: A5PDF5_9SPHN
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ID   A5PDF5_9SPHN            Unreviewed;       545 AA.
AC   A5PDF5;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Putative monooxygenase {ECO:0000313|EMBL:EDL48275.1};
GN   ORFNames=ED21_32029 {ECO:0000313|EMBL:EDL48275.1};
OS   Erythrobacter sp. SD-21.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL48275.1, ECO:0000313|Proteomes:UP000005498};
RN   [1] {ECO:0000313|EMBL:EDL48275.1, ECO:0000313|Proteomes:UP000005498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD-21 {ECO:0000313|EMBL:EDL48275.1,
RC   ECO:0000313|Proteomes:UP000005498};
RA   Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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 monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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:EDL48275.1}.
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DR   EMBL; ABCG01000007; EDL48275.1; -; Genomic_DNA.
DR   RefSeq; WP_006834181.1; NZ_ABCG01000007.1.
DR   AlphaFoldDB; A5PDF5; -.
DR   STRING; 161528.ED21_32029; -.
DR   eggNOG; COG2072; Bacteria.
DR   OrthoDB; 312624at2; -.
DR   Proteomes; UP000005498; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:EDL48275.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005498}.
FT   DOMAIN          9..220
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   545 AA;  61353 MW;  628DCD6D9E911B2B CRC64;
     MSHSPPPDYD VVIVGAGFSG IYLLYKLRQA GFDVLLVDAA EQPGGIWYWN RYPGARVDSQ
     VPLYEFSIAE VWKSWTWSER FPGWEELRAY FLHVCDTLDL WPAMRMKTRV ESAPFDEDTA
     CWRLKLDDGG KVSARFLLPA LGFASKPYIP DILGLSDFEG EWCHTARWPQ EGIDLSGRRI
     ALIGTGASGV QVAQEAASCA EQLTLFQRTP ILALPMRQEK LDADRQLREK SEYPAVFHKR
     LTTSGGFECQ SLDISALAVT EEERTTHFED LWQRGGLRFW YHNFADILTN EDANRHAYEF
     WCDKVRERIC DPTIAEKLAP DEPPHPFGTK RPSLEQNYYE IFAQDNVTLV DLNDTAITRV
     TEAGIETATG MIPCDLIVFA TSFDAGRGGL IDMNITGRGR LALAEAWKSE IKAYLGMAVA
     QFPNMLFAYG PLSPSGFSNG PTSAEIQGDW ICDFRIWLRD NRIGLFEADA LAERSWTDMV
     AQVGSMTLFP KAESWYMGAN IPGKPRQLIN FPSVSGYADL CHDVARHDYR GFIRNTLSGM
     ETAPK
//
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