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Database: UniProt
Entry: S0EMV3_GIBF5
LinkDB: S0EMV3_GIBF5
Original site: S0EMV3_GIBF5 
ID   S0EMV3_GIBF5            Unreviewed;       333 AA.
AC   S0EMV3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Related to hydroxylacyl-CoA dehydrogenase {ECO:0000313|EMBL:CCT73753.1};
GN   ORFNames=FFUJ_09429 {ECO:0000313|EMBL:CCT73753.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT73753.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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DR   EMBL; HF679031; CCT73753.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EMV3; -.
DR   STRING; 1279085.S0EMV3; -.
DR   EnsemblFungi; CCT73753; CCT73753; FFUJ_09429.
DR   VEuPathDB; FungiDB:FFUJ_09429; -.
DR   HOGENOM; CLU_009834_0_1_1; -.
DR   OrthoDB; 5402028at2759; -.
DR   Proteomes; UP000016800; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..193
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          197..250
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   REGION          304..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            148
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   333 AA;  36435 MW;  82D0BACAA6FFBB3C CRC64;
     MSDTQNKEII ALIGLGTIGL SFAALHLRYS NANLRLYDVR SDLKEHIESL LPVYLESTKK
     ENSQNDLTVE KLVADGRLLV CSSIEEVCSG ATIVQEQGPD SVDFKKSNWA QVIKYAPSNA
     HLWSSTSGIS ASRQVEDLEN KTRVLVVHPF NPPHIMPLIE VVPSPHTDPE RTQFAIDYFK
     NLGSGHRPVR INKETQGFVG NRLAFALFRE ACHLVSNDVV SVEDLDTIVE ASIAPRWAVA
     GPFKTYNSAG GTGGIGAFLH NLADTMEACW DDAGDISLKG TSATKASQGT DDGDWTDKIT
     KETEQAYGRP TAESLAQRDR NLQKVISAQP KVD
//
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