FOX2_NEUCR
ID FOX2_NEUCR Reviewed; 894 AA.
AC Q01373; Q7S8Y7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxisomal hydratase-dehydrogenase-epimerase;
DE Short=HDE;
DE AltName: Full=Multifunctional beta-oxidation protein;
DE Short=MFP;
DE Includes:
DE RecName: Full=2-enoyl-CoA hydratase;
DE EC=4.2.1.119;
DE Includes:
DE RecName: Full=(3R)-3-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.n12;
GN Name=fox-2; ORFNames=NCU08828;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 497-525 AND 604-619.
RC STRAIN=74-OR8-1A / DSM 1258;
RX PubMed=7715608; DOI=10.1007/bf00425825;
RA Fossa A., Beyer A., Pfitzner E., Wenzel B., Kunau W.-H.;
RT "Molecular cloning, sequencing and sequence analysis of the fox-2 gene of
RT Neurospora crassa encoding the multifunctional beta-oxidation protein.";
RL Mol. Gen. Genet. 247:95-104(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP PROTEIN SEQUENCE OF 487-528.
RX PubMed=1830049; DOI=10.1016/s0021-9258(18)98812-5;
RA Thieringer R., Kunau W.-H.;
RT "Beta-oxidation system of the filamentous fungus Neurospora crassa.
RT Structural characterization of the trifunctional protein.";
RL J. Biol. Chem. 266:13118-13123(1991).
CC -!- FUNCTION: Second trifunctional enzyme acting on the beta-oxidation
CC pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase
CC activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-
CC ketoacyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:32711, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726;
CC EC=1.1.1.n12;
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. Note=Catalase-free
CC microbodies.
CC -!- DOMAIN: Contains two SDR domains.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X80052; CAA56355.1; -; mRNA.
DR EMBL; CM002239; EAA32803.1; -; Genomic_DNA.
DR PIR; S54786; S54786.
DR RefSeq; XP_962039.1; XM_956946.2.
DR AlphaFoldDB; Q01373; -.
DR SMR; Q01373; -.
DR STRING; 5141.EFNCRP00000008724; -.
DR PRIDE; Q01373; -.
DR EnsemblFungi; EAA32803; EAA32803; NCU08828.
DR GeneID; 3878199; -.
DR KEGG; ncr:NCU08828; -.
DR VEuPathDB; FungiDB:NCU08828; -.
DR HOGENOM; CLU_010194_18_1_1; -.
DR InParanoid; Q01373; -.
DR OMA; LITEMWK; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0106386; F:(3R)-hydroxyacyl-CoA dehydrogenase (NAD) activity; IEA:RHEA.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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 Pfam; PF00106; adh_short; 2.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Fatty acid metabolism; Isomerase;
KW Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase;
KW Peroxisome; Reference proteome; Repeat.
FT CHAIN 1..894
FT /note="Peroxisomal hydratase-dehydrogenase-epimerase"
FT /id="PRO_0000054699"
FT DOMAIN 776..887
FT /note="MaoC-like"
FT REGION 6..230
FT /note="Short-chain dehydrogenase like 1"
FT REGION 311..523
FT /note="Short-chain dehydrogenase like 2"
FT REGION 763..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 318..342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 693..694
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 803..808
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 826
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 851
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
SQ SEQUENCE 894 AA; 96326 MW; 29758220D397AA88 CRC64;
MAEQLRFDGQ VVVVTGAGGG LGKAYCLFFG SRGASVVVND LGASFKGEGN STKAADVVVN
EIKAAGGKAV ANYDSVENGD KIIETAIKEF GRIDILINNA GILRDISFKN MKDEDWDLIF
KVHVKGSYKT ARAAWPYFRK QKFGRVINTA SAAGLFGNFG QANYSAAKLG MVGFTETLAK
EGLKYNIISN VIAPIAASRM TETVMPPDLL ALMKPEWVVP LVAVLVHKNN TSETGSIFEV
GGGHVAKLRW ERSSGLLLKA DESYTPGAII KKWDQVTDFS NPQYPTGPND FLALLEESLK
LGPNDPGEKV DFKGRVALVT GGGAGIGRAY CLAFARAGAS VVVNDLVNPD DVVNEIKKMG
GKAVGAKFSA EDGDAVVKAA IDAFGRVDIV VNNAGILRDK AFHNMDDSLW DPVMNVHARG
TYKVTKAAWP YFLKQKYGRV LNTTSTSGIY GNFGQANYSA AKCAILGFSR AIALEGAKYN
IYVNTIAPNA GTAMTKTILP EELVQAFKPD YVAPLVLALC SDKVPKKPTG GLYEVGSGWC
GQTRWQRSGG HGFPVDVPLT PEEVVKHWND IVTFDSRADH PEKASDSIEK IMANMENRVG
EGKSGAAENE HLAAIKKFTG VEGKGTEYTF TERDVCLYNL GIGAKRTDIK YIFEGNEDFE
VVPTFGVIPP FNTEMPFSFD DIVPNFSPMM LLHGEQYLEV RKYPIPTSGR LVSKGKLLEV
VDKGSAAIVK QGITTFNAET GEELFYNEMT VFLRGCGGFG GQKKPADRGA STAANKPPAR
SPDAVVEVQT TEEQAAIYRL SGDYNPLHVD PAFAKVGGFK VPILHGLCSF GIAGKAVYEK
YGKFKNIKVR FAGTVNPGQT LVTEMWKEGN KVVFQTKVKE TGKLAISGAA AELA
