ID F2GC26_ALTMD Unreviewed; 506 AA.
AC F2GC26;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:AEA98042.1};
GN OrderedLocusNames=MADE_1009520 {ECO:0000313|EMBL:AEA98042.1};
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373 {ECO:0000313|EMBL:AEA98042.1, ECO:0000313|Proteomes:UP000001870};
RN [1] {ECO:0000313|EMBL:AEA98042.1, ECO:0000313|Proteomes:UP000001870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype
RC {ECO:0000313|Proteomes:UP000001870};
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
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DR EMBL; CP001103; AEA98042.1; -; Genomic_DNA.
DR RefSeq; WP_012518368.1; NC_011138.3.
DR AlphaFoldDB; F2GC26; -.
DR KEGG; amc:MADE_1009520; -.
DR HOGENOM; CLU_022247_1_0_6; -.
DR Proteomes; UP000001870; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR InterPro; IPR033856; Trp_halogen.
DR PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR PANTHER; PTHR43747:SF4; FLAVIN-DEPENDENT TRYPTOPHAN HALOGENASE; 1.
DR Pfam; PF04820; Trp_halogenase; 1.
DR PIRSF; PIRSF011396; Trp_halogenase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR011396-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR011396-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011396-2}.
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 17..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 82
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 344
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 506 AA; 57026 MW; C5A2B6E68A6FA080 CRC64;
MQDPHNKPIK RVVIAGGGTA GWLAASLMKK VLGKAVDITL VESEAIGTVG VGEATIPPIR
LVNQVLGIDE AQFLHDTKAT IKLAIRFENW KTKGESYYHT FGAPGKSMAF CHFHHYWVKA
RQQGLKADLW DFDLNYHAAE AGRFAQINAK DPVVELPFAY HFDASLYAQY LRKLSENMGV
VRKEGKISRV QRFTDSGFIQ ALHLESGDVV EGDLFVDCTG FKGLLIEEAL GAGYDDWSHL
LPCDSAIAVP SERHEKTAPY TRSIAHDAGW QWRIPLQHRN GNGHVYSSRY ISDDQACDTL
LSNLDTKPLG DPKLIKFTTG RRRKQWYKNV VAVGLSSGFL EPLESTSIHL IQSAIVRLIQ
LFPHNGFAPS LESEYNKQSE LEFEQIRDFL VLHYTVNERT DSAFFNDMRN ITLPDSLAHK
IALFKESGNL LREQNDLFLE SSWLQVLYGQ GITPKDYHGL VNSVPEVQLN QMLTRLLEIK
KEPIAKLPTH DEYINGMVAK YKRAMS
//
