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Database: UniProt
Entry: A0A194ULV0_9PEZI
LinkDB: A0A194ULV0_9PEZI
Original site: A0A194ULV0_9PEZI 
ID   A0A194ULV0_9PEZI        Unreviewed;       315 AA.
AC   A0A194ULV0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   SubName: Full=Putative 3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KUI52640.1};
GN   ORFNames=VP1G_00158 {ECO:0000313|EMBL:KUI52640.1};
OS   Valsa mali var. pyri.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI52640.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific
RT   Adaption of Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN714666; KUI52640.1; -; Genomic_DNA.
DR   EnsemblFungi; KUI52640; KUI52640; VP1G_00158.
DR   OrthoDB; 938257at2759; -.
DR   Proteomes; UP000078576; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000078576};
KW   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT   DOMAIN       31    214       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      219    315       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   NP_BIND      35     40       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   BINDING      59     59       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   BINDING     118    118       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   BINDING     123    123       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   BINDING     145    145       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   BINDING     176    176       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   BINDING     307    307       NAD. {ECO:0000256|PIRSR:PIRSR000105-2}.
FT   SITE        173    173       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000105-1}.
SQ   SEQUENCE   315 AA;  33847 MW;  3C23F26FF2B64DFF CRC64;
     MAVSVTRVRQ IRRLLPRLRH YSSSSTPVKR LGVVGAGQMG LGIALVAAQK AQVPVTLVDN
     SQASLDKGLA FAEKLLAKDV AKERITQEQA DKARANLTPI NTLDALSEVD FVIEAVPEIP
     QLKFDIFSKL AQICPPHAIL ATNTSSISIT SIAASTTKDP KDLSASSRVV STHFMNPVPV
     QKGVEIISGL QTSQDTVDQA IAFCKAMGKI PSVSADSPGF LANRILMPYI NEAVICLETG
     VGDRDSIDAI MKNGTNVPMG PLQLADFIGL DTCLAIMRVL HEETGDSKYR PSVLLRKMVD
     AGWLGKKSGK GFYDY
//
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