ID   A0A0J8QV88_COCIT        Unreviewed;       904 AA.
AC   A0A0J8QV88;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peroxisomal multifunctional enzyme type 2 {ECO:0000313|EMBL:KMU75183.1};
GN   ORFNames=CISG_04130 {ECO:0000313|EMBL:KMU75183.1};
OS   Coccidioides immitis RMSCC 3703.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU75183.1, ECO:0000313|Proteomes:UP000054559};
RN   [1] {ECO:0000313|Proteomes:UP000054559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; DS268138; KMU75183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8QV88; -.
DR   STRING; 454286.A0A0J8QV88; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000054559; 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:UP000054559}.
FT   DOMAIN          780..890
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
FT   REGION          759..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  97346 MW;  3B2C70753EE8ACE7 CRC64;
     MSQLRFDGQT VVVTGAGGGL GKAYAVFFGS RGANVVVNDL GGSHTGEGHS SKAADVVVDE
     IRSKGGKAVA NYDSVEFGEK IIETAIKNFG RIDILINNAG ILRDVSFKNM KDQDWDLINQ
     VHTYGSYKCS RAAWPYFRKQ KFGRVINTAS AAGLFGNFGQ TNYSAAKLAL VGFTETLAKE
     GIKYNIHANV IAPIAASRMT ETVMPPEVLE NLKPEWVVPL VAFLVHSSCK ETGSIFEAGA
     GHVAKLRWER AKGALLKTDD SLTPGALLAK WDQVNNFSEP SYPTGPNDFM DLLEEGMKLP
     SSPAAKQPDF TGKVALITGA GNGLGRAYAL LFAKLGAAVV VNDLVDPEPV VQEIKQMGGK
     AVGSKASVED GAAVVKPAID AFGRIDILVN NAGILRDKAF TNMDDSLWNP IINVHLRGTY
     SVTKAAWPYM LKQKYGRIVN TTSTSGIYGN FGQANYAAAK LGILGFSRAL ALEGAKYNIL
     VNTIAPNAGT QMTRTVMPEE VVQAFKPDQV APIVALLCSD MVPQPATKGL YECGSGWFGR
     TRWQRSGGHG FPIDVELTPE AVAAMWSKIT NFDDGRADHP EDGQAGFKSI MENMSNRSGG
     SAAKGSDENQ QILDAITAAK GMKAEGTSFD YTDRDVILYN VSLGAKRTQL PLVYENDDNF
     QPLPTFGVVP WFNTDIPWNM GEIVANFSPM MLLHGEQYLE IKKFPIPTAA KTISYPKLID
     VVDKGNAAIV VNGYITKDAN TGEDLFYNES TMFIRGSGGF GGPSKPTARR PAGATAAYKP
     PQRKPDAVIE EKTSEDQAAL YRLNGDRNPL HIDPEFSKVG GFKIPILHGL CSMGISGKHV
     FSKFGAFKNI KVRFAGVVLP GQTLRTEMWK EGNFVLFQTT VVETGKPAIA GAGVELVSDK
     ASKL
//