ID   F2ST18_TRIRC            Unreviewed;       905 AA.
AC   F2ST18;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=MaoC-like domain-containing protein {ECO:0000259|Pfam:PF01575};
GN   ORFNames=TERG_05621 {ECO:0000313|EMBL:EGD89378.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89378.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG700653; EGD89378.1; -; Genomic_DNA.
DR   RefSeq; XP_003233747.1; XM_003233699.1.
DR   AlphaFoldDB; F2ST18; -.
DR   STRING; 559305.F2ST18; -.
DR   GeneID; 10372378; -.
DR   VEuPathDB; FungiDB:TERG_05621; -.
DR   eggNOG; KOG1206; Eukaryota.
DR   HOGENOM; CLU_010194_18_0_1; -.
DR   InParanoid; F2ST18; -.
DR   OMA; WATKVHT; -.
DR   OrthoDB; 2140828at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase 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:1901576; P:organic substance 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; 2.
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:UP000008864}.
FT   DOMAIN          781..891
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
SQ   SEQUENCE   905 AA;  97491 MW;  B293BEC2EDCC75A0 CRC64;
     MSLRFDNQVV VVTGAGGGLG KAYALYFASK GAGVVVNDLG VSHSGEGQSS KAADVVVEEI
     KAAGGKAVAN YDSVEFGDKI IDTAIKTFGR IDILINNAGI LRDVSFKNMK DQDWDLIDKI
     HLFGAYKCAR AAWPHFRKQK FGRVINTTSA AGLFGSFGQT NYSAAKLALV GLTETLAKEG
     LKYNIHSNAI APIAASRMTE TVMPPELLAN LKPEFVVPIV AYLVHSSTTE TGSIFEAGAG
     HVAKIRWERS KGALMRADDS FTPGALLKRW EDVNDFSKPT HPTGPADYVE LIQESMKLPA
     NPPAEQPDFT GKVALVTGAG AGLGRSYALM FAKYGASVVV NDLMDPEPVV QEIKKAGGKA
     VGSKASCEDG PAIIKTAIDN FGRIDIVINN AGNLRDKAFT NMDDKLWTSV VNVHLRGTYS
     VTKAAWPYFL KQKFGRIVNT TSTSGIYGNF GQANYASAKL GILGLSRTLA LEGAKYNIRV
     NTIAPNAGTD MTRTIMPEEL VQALSPNQVA PLVVLLCSEL LPEPTTKGLY ECGSGWTGKT
     RWQRSGGHGF PVDAELTIED VAKTWSKIID FDDGRADHPD DTLAGAESIM ANINNKVGES
     KKEEAPKGGD QTILDNISKA KEMKAEGTAF DYADKDIILY SLSVGAKRTQ LPLVYENHDE
     FQALPTYGVI PWFNTAVPWN LGDVVANFSP MMLLHGEQYL EIRKYPIPTE AKTITYPKLI
     DVIDKGNAAI VVMGYTTKNA KTGEDLFYNE STMFIRGSGG FGGSNKSTAS RPAAATAAYK
     PPQRKADAVV EEKTGEDQAA LYRLNGDRNP LHLDPDFSKM GGFKTPILHG LCSLGISGKH
     IYEKYGAFKN LKVRFAGVVL PGQTLRTEMW KEGNVVVFQT TVVETGKPAI AGAGVELVSN
     PKGKL
//