ID A0A093UQQ7_TALMA Unreviewed; 605 AA.
AC A0A093UQQ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Zinc-type alcohol dehydrogenase-like protein PB24D3.08c {ECO:0000313|EMBL:KFX42280.1};
DE Flags: Fragment;
GN ORFNames=GQ26_0460190 {ECO:0000313|EMBL:KFX42280.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX42280.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX42280.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX42280.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- SIMILARITY: Belongs to the CybS family.
CC {ECO:0000256|ARBA:ARBA00007294}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX42280.1}.
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DR EMBL; JPOX01000046; KFX42280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093UQQ7; -.
DR HOGENOM; CLU_552304_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05288; PGDH; 1.
DR CDD; cd03496; SQR_TypeC_CybS; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR PANTHER; PTHR43205:SF7; PROSTAGLANDIN REDUCTASE 1; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF05328; CybS; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 112..429
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT NON_TER 605
FT /evidence="ECO:0000313|EMBL:KFX42280.1"
SQ SEQUENCE 605 AA; 66417 MW; E9DEA085661103BE CRC64;
MRRTEGDGVH PHARAVRNLP RSIGYDRFEQ QGEPPYPYHI CCSKVGRISG KQNLTKAWLE
YKMPPLPSWT KVLILVASSL VIHTYTYTET SIMPDNRALF FSSVPSGLPV VGKDLTLESV
PYPEEVSENG IIVKNVYASL DPYMRGRMRA PEVKSYATPF ELHKPIFNRQ IAQVTKSNNA
NFKEGDLVIG MLPFQEYVAL NGDQVAELQP LQNPLGLEDI RDFLGALGMP GLTAYSSLYE
IGKPKKGDTI FVSAASGAVG QLVGQLAKHE GLKVIGSVGS DEKLEFILKD LGFDAGFNYK
KESPAQALQR LAPEGLDIYY DNVGGDHLEA SLDAMKDYGR VILCGLIAVY NQKPEEIYPL
GNYGQILWKR LTVRGFLVGD KGMGDKYDDE HQKRVSKWIQ EGIFKAVNWE VEGIEQAADG
FTSTSSLTTD NSRLLDVAYS ACRPDPLHSS NSPATMAAFI RPSSGAMMGT IMRVPAVYSA
KSAPLALTLV RQAQVTQFHS SAKREILTPL PQVVKGTMND AAPVPHTSPS HGSYHWTFER
LIAAGLVPLT IAPFVGGSLN PVMDSILAAG LVLHSHIGFQ ALIIDYLPQQ RVPKTLALFK
WGLRA
//
