ID A0A1L9NKR9_ASPTC Unreviewed; 901 AA.
AC A0A1L9NKR9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=MaoC-like domain-containing protein {ECO:0000259|Pfam:PF01575};
GN ORFNames=ASPTUDRAFT_157874 {ECO:0000313|EMBL:OJI89827.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI89827.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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}.
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DR EMBL; KV878177; OJI89827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9NKR9; -.
DR STRING; 767770.A0A1L9NKR9; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_157874; -.
DR OMA; WATKVHT; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000184304; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:UP000184304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 776..887
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
SQ SEQUENCE 901 AA; 97098 MW; A29A8AA866FC4CDF CRC64;
MSELRFDNQT VVVTGAGGGL GKAYALFFAS RGANVVVNDL GGSHSGEGKS AKAADVVVDE
IRAAGGKAVA NYDSVENGEA IIETAIKNFG RIDVLLNNAG ILRDISFKNM KDQDWDLIYR
VHTYGAYKCA RAAWPHFRKQ KYGRIINTAS SAGLFGSFGQ ANYSAAKLGQ VGFTETLAKE
GAKYNIIANV IAPIAASRMT ATVMPPEVLE NLKPDWVVPL VAALVHSSNT TETGGIYEVG
GGHVAKLRWE RAKGALLKTD ASLTPGAIAR KWNDVNDFSK PDYPTGPADF MGLLEDGLKL
PSAQAGEEPN FKGKVALVTG GGNGLGRAYC LLFAKYGAAV VVNDLVDPEP VVQEIKKMGG
QAVGNKASCE DGENVVKTAI DTFGRIDILI NNAGILRDKA FTNMNDDLWN PVLNVHLRGT
YKVTKAAWPY MLKQKYGRIV NTASTSGIYG NFGQANYAAA KLGILGFSRT LALEGAKYNI
KVNTIAPNAG TNMTRTIMPE EMVQAFKPDY VAPLVALLCS DIVPEPSTKG LYECGSGWFG
RTRWQRTGGH GFPVDVKLTP EEVLKHWQKI TNFDDGRADH PEDGQAGSEK IMANMSNRSG
GDSEGGNNIL QAIEKAKQAT TDGTSFDYED RDVILYNLSV GAKRTDLPLV YENNEHFQAL
PTYGVIPWFN TANPWNMDEI VANFSPMMLL HGEQYMEVRK FPIPTAAKTL TYPKLIDVVD
KGNAALVVSG YTTKDAKTGE DLFYNESTVF IRGSGGFGGS PKPTAPRPKA AVASYKAPQR
KPDAVVEEKT SEDQAALYRL NGDRNPLHID PEFSKVGGFK TPILHGLCSL GVSGKHVFST
YGAFKNLKVR FSGVVLPGQT LRTEMWKEGN VVIFQTTVVD TGKPAITGAG AELLEGAKAK
L
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