ID C6VZM2_DYAFD Unreviewed; 464 AA.
AC C6VZM2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Amine oxidase {ECO:0000313|EMBL:ACT93500.1};
GN OrderedLocusNames=Dfer_2278 {ECO:0000313|EMBL:ACT93500.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT93500.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT93500.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; CP001619; ACT93500.1; -; Genomic_DNA.
DR RefSeq; WP_015811752.1; NC_013037.1.
DR AlphaFoldDB; C6VZM2; -.
DR STRING; 471854.Dfer_2278; -.
DR KEGG; dfe:Dfer_2278; -.
DR eggNOG; COG1231; Bacteria.
DR HOGENOM; CLU_004498_0_4_10; -.
DR OMA; PIHWAGT; -.
DR OrthoDB; 56323at2; -.
DR Proteomes; UP000002011; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF1; AMINE OXIDASE [FLAVIN-CONTAINING] B; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002011}.
FT DOMAIN 18..458
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 464 AA; 52443 MW; E3C71ABF232DA520 CRC64;
MQRDKFDTQV VIVGAGYSGI AAAKRLYEKN VEFMVLEARD RIGGRVLTYP IQHDMNIELG
AQWIGPGHDL MYEWIAEAGY HTFDTFDHEH HIYEHKGRQS FYTSAEEGPD MNFVYRAGFR
AVLGLSDAFA RLTWNNFPNG LSEILDKYTV QDFFKCIKPL TGRSYFGISK GFEISSAQRS
GDMSLLHALH NIYSAGEFRK IIKVDGGAQQ SIIREGSQNL LSNISAKFSD RIRFNQPVMK
IAHTDTGVRI FTSNESVYAQ KVILAIPPAH LLPIDLGSNP LFEKRKSLVE KLKLGTPIKC
FAIYDRPFWR ERRPFYRERA LSGQVVTDRY PFVASYDCSP GTGPGVLLFF VKEKTTGEFT
SRSMEERKAL LVDQIVRLYG PEGANILAYK DHIWNDIEER WSGGGYAASF PKGLWSQTGK
DFRNPIGNIH WAGSEMATKW YGYMEGAIQA GYHAADEVNA SLSS
//