ID I4B2K2_TURPD Unreviewed; 455 AA.
AC I4B2K2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Amine oxidase {ECO:0000313|EMBL:AFM11509.1};
GN OrderedLocusNames=Turpa_0858 {ECO:0000313|EMBL:AFM11509.1};
OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS (Leptospira parva).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Turneriella.
OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM11509.1, ECO:0000313|Proteomes:UP000006048};
RN [1] {ECO:0000313|EMBL:AFM11509.1, ECO:0000313|Proteomes:UP000006048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC {ECO:0000313|Proteomes:UP000006048};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL Submitted (JUN-2012) 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 flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; CP002959; AFM11509.1; -; Genomic_DNA.
DR RefSeq; WP_014802027.1; NC_018020.1.
DR AlphaFoldDB; I4B2K2; -.
DR STRING; 869212.Turpa_0858; -.
DR KEGG; tpx:Turpa_0858; -.
DR HOGENOM; CLU_004498_0_4_12; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000006048; 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; FLAVIN-CONTAINING MONOAMINE OXIDASE B-RELATED; 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:UP000006048}.
FT DOMAIN 24..451
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 455 AA; 49212 MW; 9EEB63B689C3A171 CRC64;
MKGNKLSRRS GARSVDVVVI GAGFAGLTAA RALEAQGLKV QVIEARDRVG GRSRPGKLFG
RTIDTGGQWV GVGHERLTRL VHEAGAELVP QYSVGKKLVQ INNKTRYYSG LIPPVSVRAL
IEMQFALWRL TALQRKIDPK VPWQSTLANL DTQTVADWQR RWLRSDGAQA LFDIGVRAIF
CAKPGQLSML HFLTYLRANG SFNYLASAEG GAQAATVKGG MHQLSVHLAK KLQQKILFGA
PVQKITQSSK GVVVTHSRGN IQAKRVVLAV APALARKIEG DAMTTARRRL GERMPMGSVI
KCLIAYKRPF WREQGFTGEF VSNTAGFSPM FDASPADGSC GILVGFFDGP TAVRWSSDAD
GRRREVIRSV VAAFGAEGEN PVDYVDHDWI TDPFSEGCYV GLPAPGALTE LGASLRAPHG
RVHYAGTETA SEWIGYIEGA IESGERAAIE VCAAL
//
