ID C8VG00_EMENI Unreviewed; 562 AA.
AC C8VG00;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=FAD/FMN-containing isoamyl alcohol oxidase MreA (AFU_orthologue AFUA_6G03620) {ECO:0000313|EMBL:CBF81578.1};
GN ORFNames=ANIA_11243 {ECO:0000313|EMBL:CBF81578.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF81578.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001305; CBF81578.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VG00; -.
DR EnsemblFungi; CBF81578; CBF81578; ANIA_11243.
DR VEuPathDB; FungiDB:AN11243; -.
DR eggNOG; ENOG502R8I5; Eukaryota.
DR HOGENOM; CLU_018354_4_2_1; -.
DR InParanoid; C8VG00; -.
DR OMA; TAQYGGW; -.
DR Proteomes; UP000000560; Chromosome V.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878:SF179; FAD_FMN-CONTAINING ISOAMYL ALCOHOL OXIDASE MREA (AFU_ORTHOLOGUE AFUA_6G03620); 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..562
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002993392"
FT DOMAIN 114..293
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 562 AA; 60878 MW; FDC081B6CF2EB985 CRC64;
MLGLSTGLAL LTSFISLFPI NGDCSCRCMP GDACWPDRAT WSRFNQSIDG RLIATVPLGT
PCHGSTYNEA VCDALRAEWT LPELHYGTSS SIMAPFFANS SCDPFHPVDK PCTLDNYIVY
AVNVSKPEHI SKAIQFTTKY NIRTVIRNTG HDYNGKSTGA GALGIWTHHL KDIEVKDWKD
SNYKGKAIKL GAGVQGLEAY EATDAQGLEV VGGECPTVGI AGGYTQGGGH SALASVHGLA
ADQVLQWEVI DGKGRFITAT RDNEYSDLFW ALSGGGGGTY GVVWSMTSKA HPGTPVSGLN
LTFTNAGISQ DTFYDAVGLY HATLPSLVDA GTMSIWYFTN TSFSLTPLTG PNIPVAKLKQ
LLQPFTDGLT DLGITYNLYA EQFPSYLAQF NGMQAAIEVG IAQYGGWLIP RSVVIENNAA
LTDGYRHITE SGATFIGVGL NVSKAVSGDV HNAVLPAWRD ALIDTTLTTP WEWNADEEML
AQQRKMTEDY IPTLMALAPD SGAYMNEGDF RQPNWKEAFY GSNYDTLRKV KAKYDPNDVF
YASKAVGSDE WTISGNGRLC RA
//
