ID B6QPN8_TALMQ Unreviewed; 967 AA.
AC B6QPN8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 13-SEP-2023, entry version 69.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase, putative {ECO:0000313|EMBL:EEA20031.1};
GN ORFNames=PMAA_038980 {ECO:0000313|EMBL:EEA20031.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20031.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995904; EEA20031.1; -; Genomic_DNA.
DR RefSeq; XP_002151031.1; XM_002150995.1.
DR AlphaFoldDB; B6QPN8; -.
DR STRING; 441960.B6QPN8; -.
DR VEuPathDB; FungiDB:PMAA_038980; -.
DR HOGENOM; CLU_017201_2_0_1; -.
DR OrthoDB; 1952864at2759; -.
DR PhylomeDB; B6QPN8; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
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 InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR48075:SF3; 3-HYDROXYACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 22..63
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 118..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 108967 MW; CBD3EECD4BD8CDB3 CRC64;
MKDFTSSSVK GHLVPRRTQF SSCDACRKSR VACDAMKGRS ALTSPTWMNS CTRCQNRGRH
CTFEVANSLN YKGANMLIKF QWIEKAALPN KMFTSLHRQR QKRVRHRKVW SVTEVPSRIG
ADTPRGHQSK GDNPPGWKRL VVTDGTTPSY DRQNPVSTPG DTHEWLREIY EGIFEDVFGS
WLGNYSCPYV FRDNGCQDPK QLALSVSISR LCQECDYWMK RVQGQGMNLS EEGESPDEID
SDRQINHSLS CAVSAFSARW LPLKESSALS ELSVMDIVES LWREVRRDIL RVINRPCYRS
ALTLFLFALT PIPARVSEEE ENDGIPAQFC VQVALQQVLT LRALQKSLEF NGSKVTSISS
ATLPNATTSP APVTRDFLGI ESMIYWAAMT FDTSSSLTLN TKSLLSPGLS LGLEQEPSWR
LVRTCTNVFH EETEAWRAQG IHITEERANQ IIASAASWKL FVWKAAALVK EALREGREDE
TVQVAFDTAV DAINQYSLTY HDLLIACERR IQFFSHKTKL RWYELILHYN LSILVMLDAV
EIAGRMDLLE KLKVVKADAE GSLFNCLIFG LNNHYLVPRR PAGEEQHGIQ LAEEDGRAAA
LELTRKVPLI AIDPYPHHVV AGVRILWKAV ERDLENDWLD YGVAEHMQDT MLNALKLLPQ
ASKSVQTVRQ QAEASFIRNS KMARSKFLRE AVVILGAGTQ GRRLAYMWSS TGKPVHLIDR
QEKQLSEGVE YVQQLRSSPS AISKNWGNIT TSSPHGLSTA LQKAWLAIEC VPENIDLKRT
VIGELDALAP EQTIIASNSS SYVIGEIIEP LSLKCPSRIL SAHCYWPPET PAIEIMGHDK
TDPFVLEQML SQCKEHGFSP YHVKATSIGY IYNRIWAAIK RETLLTLHEG VATPKEIDAI
FKDVLKTPKG PCELMDLVGL DVVLDIERHY ADSRKDLPLE PREYLGKMIE NGKLGLKNGR
GFYNYIP
//
