ID N1RU30_FUSC4 Unreviewed; 598 AA.
AC N1RU30;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Choline dehydrogenase, mitochondrial {ECO:0000313|EMBL:EMT67682.1};
GN ORFNames=FOC4_g10005789 {ECO:0000313|EMBL:EMT67682.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT67682.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KB726570; EMT67682.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RU30; -.
DR STRING; 1229665.N1RU30; -.
DR HOGENOM; CLU_002865_6_0_1; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..598
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004111795"
FT DOMAIN 102..125
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 282..296
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 534
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 577
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 104
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 598 AA; 63975 MW; EBE084891F0F5EEF CRC64;
MLVKLHLWFS LAAAAVAAPS KDAYDYIVVG GGTAGVAVAA RLSEGLPSAN ILLIEAGPAA
HDEPKINIPG MKGSTLGTKY DWNFTTVPQT GANNRVWPIN RGKVLGGSSA LNLMTYDRAA
VAEYDAWQAL GNPGWNWKTM IKAMMKSETF TGKNTATYGS KGVGDSGPVK AVVNRIIPKH
QESWIPTLNK LGVRKNLESL GGDPLGVMYQ PSSIDPSNYN RSYSANAYTE ISGPNLEILA
DTIVAKINVS GPAAKKKAIA TGVTLQDGTY VKARREVILS AGSIQSPGLL EQSGIGSKSV
LSAAGIKQII DLPGVGENLQ DHLRVMTSYQ LKPEFLSFDA LRSNATFAAE QLALWNAGKR
SLYDYTGSAY TFSTWKQALG SDAKLVSLAK DAAGKDASKV DKKKLDFLKD SSVPQVEVIF
SDGYTGVKGY PAATSPLFGK GFVTLIGVVM HPLSRGSVHI NPSDPAGKPT INPNYLSNPH
DVEAVFQTVK YNRKIANTEP MRSIWEDEYE PGLDVKTDEQ IKDYVLRTTL SIFHPSGTCA
MLPKADGGVV DAKLKVYGTE NLRVVDASVI PLLISAHIQT AVYGIAEIAA ELIIKDAK
//
