ID R9P6E5_PSEHS Unreviewed; 2303 AA.
AC R9P6E5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=PHSY_004567 {ECO:0000313|EMBL:GAC96983.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC96983.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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DR EMBL; DF238808; GAC96983.1; -; Genomic_DNA.
DR RefSeq; XP_012190570.1; XM_012335180.1.
DR STRING; 1305764.R9P6E5; -.
DR GeneID; 24109849; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_229901_0_0_1; -.
DR OrthoDB; 1448718at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR11695; ALCOHOL DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11695:SF294; RETICULON-4-INTERACTING PROTEIN 1, MITOCHONDRIAL; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000014071}.
FT DOMAIN 1972..2300
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 47..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1779..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2303 AA; 242347 MW; 90D0F8AEDECF1B8A CRC64;
MRIACHQAAA CLVSDFGIFF RCSDADAARL SRNPSIMSKH SFMDTILNRP SQRYTEPQQA
KPSRNARYQT PHDLPNAPNK PDSILAGTMF TGAGPGALNQ SNGNNYSRAP SVMSGKSNTS
RFSIFRKKNR APSVSGGSVY YDGASSVAPT DITSTARKGR WWESGTRNTY TSRPPSIAGS
VFSEPEASGP PGFPRISDSM HASAPARGAR SDYGGGSSNR KRYSSQPGVP VTYQPASKAS
MSSMKRQSGV TPLGQQAPNL MRQASSASLV RSQSNATSNT DLNRPVSPAA SMGRRQSQTR
LAPSASSDWN SFVKSMSGTE VAKTWEQMPT LAPKPPRTSE KRSSVVANRI RKELEQDAQY
QQVQRDPGVV QQDLLARAAS QVIGAMPPTP ASPPSEAHTA PLRLQPGQVV MPISPVASNS
SLNVAHYPSS MALQASTAVN GAGSQASVNV PQNVATVTVA QSPQPPQQYV HPQAVAHPSN
GAVPSDPSHQ STGAAPPLAK PQQAMPASIP THRASASPPL QQQAAPIPTQ TYAPVAVPAP
RVVAQAPTSP PSVAAVLPPA ADGAVPQVPV PSVQPSAPAA TPTTTAQYLA DRVNEQESAG
EQADSREVSS DESEDSDDTS SEEGLVGGGQ PTLDVVAEED EELSSVGGHQ YHHEMRSRQS
AKGKGLSRNY GDYEARLHSR HASATSQQED VREGELPVAP SGVSIQVTDA RDLPISATAS
EKTENPTVHE APAVAPALAM GPPQLGATDR PKLVSRASEM SDYQSAASDS GTATKQDRDQ
DDEDEGDADA AASLARAKIG TKTSRESMST DAASIAPSQR QSVRTTRSSM PPTAQRRLSE
LSLGASFAAS GILRRPESTR RRTGGSDSGA DLSDDDADLR AEALAEQDRL RKMNVGEDFF
GPSLSTILDK FGGSTSMDSS VSKVESRHER PSVPATSASE IHAEAQQVIN EVRQNRADAT
SEGKKRNSTD TAGMAPSVAA VWLLNQAQST NDSSPARAMS DEAGDETITS SILRASAANN
VASPPVTDSP ERPKVSVLNR PRPTPKRPRE MGGVSIAEGR LESEPPLEPV TVEDTRSTLP
ISVSQTSMQS VDVSTGSVNS DSATPTKAST PIASKDTPSP SKSALKPKSS RSLADTLFTL
SFRSPSKDKK EKKDKKKKEK EEKKERKEKG KHSRKVSVDS IGSASIQSER SSTVGSDSAM
SSPSAKVLGK QRIADNANTS TAPPAAITTQ QQNGMVPSET VNTFATPPQS MANLQGMAGA
ATSPEKFHTA HDLKALADTS IPVYPTETVQ APLMPNGAAT ADARPEHQRQ LSQQINSMDG
FGSFALPQLD QRKATAMPAV NGTTKKEEAV EPSAPADASP APSLSQNASV NGVGNGSSSV
PTLSQASIAS TALTSPDSEA APQAIAAERE MPQPALAVAS SSPLEASEKK LPMPPPPQPE
EVMARTIEDQ TPTGKPIAAP GVGINLIPPT PPALESRDSF TSSQVPGTPT IEEYDEYITP
QRPSLMSRSS SQRTAVRADS KPDGASEGLS RSRSMAPARK GMWTEYKGKG LSLPPGLVAT
TIDSSALRRM STQDKKAPSQ PVAAAASSAA TPALPAAPAL AQNVVTAPLP LLDSPARPAR
STPSPSPKSR RSSGSLGGSP QRSSPVHTSP SMNRIMADAP PVPQIPAGYQ APGSVSSSPS
RPYAYSGATS EHDWDSRSAS PAPSAVPSQS GRSVGSHVSS SVHSASYRSS PRPEFTYVNH
HELSPYAKKM RSLSPSPAMP TLSQTGNRHS LMSAINEWES QVPEPEAPVV GLSPYPSRPV
SPSPSPYPTL PASTVSRSSS VISSVSSPAV VRNAPLGAST NQYLSPPIAR SRMSADELST
VSESAIESLN AGSVVGRPSG PPSASSSSPS ASQSALSLSS TVQTSMPTVP TSYRPNKDPK
RFSTNADDLL NSRTTMQTVA VTSGAFATRS KSVRRKKSVD LNGNEVPEHL QDDLAQTTLS
VTAHTPPPRK IGSHQVLVQV IAVAIDEMDK LLLREKVRAE NAFGFVPGRS FCGRIVECGY
EVKKMRKGDV VFGLQDSRKS GALAEFMVVD HNRICHAPSD CLTTEQIAAL PSAGVMAHQL
IQNHCSQLQR GARVLILNAH DGIGLLTMQE SVGLGLVIVA QCPPSISDGV AVCQANGAHE
VVIGEPLWAI NSLHESSFDL IVDTVGGRKI YDASRRILGT DGQFCTCFGD EHGTTNPNLR
SHLRSLRRAF FKKDKKNIGY EWVGVDTAED CKEALEAVKR AAEGGNICPR LRSVLPFADA
GRAFDGERRN GDDEPGAIVV RVS
//
