VAO15_MYCTT
ID VAO15_MYCTT Reviewed; 574 AA.
AC G2QDQ9;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=VAO-type flavoprotein oxidase VAO615 {ECO:0000312|EMBL:AEO58370.1};
DE Flags: Precursor;
GN ORFNames=MYCTH_2305637 {ECO:0000312|EMBL:AEO58370.1};
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2] {ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-47; ASN-105; ASN-129; ASN-211; ASN-310 AND
RP ASN-438.
RX PubMed=29303991; DOI=10.3390/molecules23010111;
RA Ferrari A.R., Rozeboom H.J., Vugts A.S.C., Koetsier M.J., Floor R.,
RA Fraaije M.W.;
RT "Characterization of two VAO-type flavoprotein oxidases from Myceliophthora
RT thermophila.";
RL Molecules 23:0-0(2018).
CC -!- FUNCTION: Probably oxidoreductase that, when reduced, rapidly reacts
CC with molecular oxygen, a hallmark of flavoprotein oxidases. A large
CC panel of alcohols, including carbohydrates, steroids and secondary
CC alcohols were tested as potential substrates, but none has been
CC identified so far. {ECO:0000305|PubMed:29303991}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:29303991};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000269|PubMed:29303991};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G2QG48}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000269|PubMed:29303991}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; CP003004; AEO58370.1; -; Genomic_DNA.
DR RefSeq; XP_003663615.1; XM_003663567.1.
DR PDB; 6F72; X-ray; 2.00 A; A=1-574.
DR PDB; 6F73; X-ray; 2.22 A; A/B=1-574.
DR PDBsum; 6F72; -.
DR PDBsum; 6F73; -.
DR AlphaFoldDB; G2QDQ9; -.
DR SMR; G2QDQ9; -.
DR iPTMnet; G2QDQ9; -.
DR EnsemblFungi; AEO58370; AEO58370; MYCTH_2305637.
DR GeneID; 11509727; -.
DR KEGG; mtm:MYCTH_2305637; -.
DR VEuPathDB; FungiDB:MYCTH_2305637; -.
DR eggNOG; ENOG502R8I5; Eukaryota.
DR HOGENOM; CLU_018354_4_2_1; -.
DR InParanoid; G2QDQ9; -.
DR OrthoDB; 827142at2759; -.
DR Proteomes; UP000007322; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..574
FT /note="VAO-type flavoprotein oxidase VAO615"
FT /id="PRO_5003435503"
FT DOMAIN 120..299
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29303991,
FT ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29303991,
FT ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29303991,
FT ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29303991,
FT ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29303991,
FT ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29303991,
FT ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT DISULFID 28..572
FT /evidence="ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT DISULFID 64..77
FT /evidence="ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT DISULFID 108..118
FT /evidence="ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT DISULFID 450..476
FT /evidence="ECO:0007744|PDB:6F72, ECO:0007744|PDB:6F73"
FT CROSSLNK 157..222
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000269|PubMed:29303991"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:6F72"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:6F72"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:6F72"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:6F72"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 346..356
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 360..376
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:6F72"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 426..439
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6F73"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 488..500
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 502..508
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 527..532
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 536..546
FT /evidence="ECO:0007829|PDB:6F72"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:6F72"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:6F72"
SQ SEQUENCE 574 AA; 61962 MW; 5E01540784C74C73 CRC64;
MPASLLRFLA LAGTAVGLTT NHNHSPSCRV LPGDAAWPSS RDWAKLNKTL NGHLIATVPQ
ASVCHKSPFG QYDAQACEEL KSSWDISTIT HVNAPGDVLS QNFQNYSCVP FTDPSQPCQL
GNYPSYVVNV TGAADVQAAL KFAQKHNVRI VIKNTGHDYL GKSTGKGALS LWMHNLKSTK
FIKNYKAPYY KGPAAKLGAG VEGFEAYAMA NSTGHRIVGG TCPTVGIVGG YTQGGGHSIL
SSSYGVAADN VLEWEVVTAD GRHLVATPTR NSDLYWALSG GGGGTFAVVL SMTARLHRDG
IVGGTLLGFN DSAVGNEVYW EAVAAFHALL PDFLDGGNSF TYSVGNNSLT AYGTMPGADR
DAVDRLLRPF LDDLASRGIT PVVQPRVSTN YYDHFFTYLG PAPYGNAAYF PFTNSRIIPR
SLVTDPKSNA VVTDLFRNIS QVPAFSPFYC DSFSVADKPH PANSLHPAWR TGMLLCAPAG
SWDWDASPEE MAARDRYAAE TLQPMMDAAT PGGSVYLNEA NHLYANWKES FYGDNYARLL
RVKKKYDPDS VFYVKTGVGS EVWDVDATGR LCRA
