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Database: UniProt
Entry: Q4W9S4_ASPFU
LinkDB: Q4W9S4_ASPFU
Original site: Q4W9S4_ASPFU 
ID   Q4W9S4_ASPFU            Unreviewed;       899 AA.
AC   Q4W9S4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Peroxisomal multifunctional beta-oxidation protein (MFP), putative {ECO:0000313|EMBL:EAL84539.1};
GN   ORFNames=AFUA_4G03900 {ECO:0000313|EMBL:EAL84539.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84539.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84539.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL84539.1}.
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DR   EMBL; AAHF01000016; EAL84539.1; -; Genomic_DNA.
DR   RefSeq; XP_746577.1; XM_741484.1.
DR   AlphaFoldDB; Q4W9S4; -.
DR   STRING; 330879.Q4W9S4; -.
DR   EnsemblFungi; EAL84539; EAL84539; AFUA_4G03900.
DR   GeneID; 3503920; -.
DR   KEGG; afm:AFUA_4G03900; -.
DR   VEuPathDB; FungiDB:Afu4g03900; -.
DR   eggNOG; KOG1206; Eukaryota.
DR   HOGENOM; CLU_010194_18_0_1; -.
DR   InParanoid; Q4W9S4; -.
DR   OMA; WATKVHT; -.
DR   OrthoDB; 2140828at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd03448; HDE_HSD; 1.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          774..884
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
FT   REGION          754..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  96808 MW;  AF17A684FE829920 CRC64;
     MSELRFDNQT VVVTGAGGGL GKAYATFFAS RGANVVVNDL GVSHSGEGAS SKAADVVVEE
     IRAAGGKAVA NYDSVENGEA IIETAIKNFG RIDVLINNAG ILRDVSFKNM KDQDWDLINK
     VHTYGAYKCA RAAWPHFRKQ KYGRIINTAS AAGLFGNFGQ ANYSAAKLGQ VGFTETLAKE
     GAKYNIIANV IAPIAASRMT ATIMPPEVLE NLKPDWVVPL VAVLVHPSNT TESGSIFEVG
     GGHMAKLRWE RAKGALLKTD ASLTPGAIAR KWKDVYDYSQ PEYPIGPADF MTLLENGMKT
     PSAPAGEEPD LKGKVALVTG GGNGLGRSYC LLFAKLGASV VVNDLVDPEP VVQEIKKMGG
     KAVGNKASCE DGDAVVKTAI DAFGRIDILV NNAGILRDKA FTNMNDDLWN AVINVHLRGT
     YKVTKAAWPH MLKQKYGRIV NTTSTSGIYG NFGQANYAAA KLGILGFSRA LAIEGAKYNI
     KVNTIAPNAG TNMTRTIMPE EMVQAFKPDY VAPMVALLCS DMCPEPSSKG LYECGSGWFS
     STRWQRSGGH GFPVDVKLTP ETVLKNWKQI TDFDDGRADH PQDSQAGTEK VMANMSNRSG
     GEGGNNILAN IEKAKQATTE GTAFDYIDRD IILYNLSVGA KRTDLPLVYE NNEHFQALPT
     FGVIPWFNTA TPWNMDDIVA NFSPMMLLHG EQYMEIRKFP IPTEAKTLTY PKLIDVVDKG
     KAALVVAGYT TKDAKTGEDL FYNESTVFIR GSGGFGGSPK PTASRPKGAT AAYNPPKRQP
     DVVIEEKTSE DQAALYRLNG DRNPLHIDPE FSKVGGFKTP ILHGLCSLGI SGKHVFNKFG
     AFKSLKVRFA GVVLPGQTLK TEMWKEGNTV IFQTTVVETG KPAILGAGAE LLEGAKAKL
//
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