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Database: UniProt
Entry: A0A0F0ID66_ASPPU
LinkDB: A0A0F0ID66_ASPPU
Original site: A0A0F0ID66_ASPPU 
ID   A0A0F0ID66_ASPPU        Unreviewed;      1288 AA.
AC   A0A0F0ID66;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   SubName: Full=FCB2FMN like protein {ECO:0000313|EMBL:KJK64707.1};
GN   ORFNames=P875_00011095 {ECO:0000313|EMBL:KJK64707.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64707.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK64707.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:KJK64707.1}.
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DR   EMBL; JZEE01000389; KJK64707.1; -; Genomic_DNA.
DR   STRING; 1403190.A0A0F0ID66; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR   CDD; cd02922; FCB2_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR003710; ApbA.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR43791:SF26; ALLANTOATE TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G09470)-RELATED; 1.
DR   PANTHER; PTHR43791; PERMEASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        830..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        871..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        901..919
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        962..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        993..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1055..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1093..1116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1128..1147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1159..1180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1187..1208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1220..1241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..77
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          101..458
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   DOMAIN          834..1247
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
SQ   SEQUENCE   1288 AA;  143002 MW;  1E14C05B4D619C91 CRC64;
     MRLTRAEVEG HNSKASCWVA IHGSVYDVTD FVDSHPGGPN AILRCAGKDA TEDFDSVHEQ
     EILTRSLAPS ALRGHIEPGT LVKSSDINET RIPNKDASLP PPLSSLLNLH DFEIVAEKHL
     PPNAWAYYAS GAEDEISKRQ NSKAFQKVSL RPRILRSIPA VDTTTTILGK QVSLPVYMSA
     VGIAKLAHPD GERALAAAAG KEGLAQVLAN GANNVIESVM DARTSSEQPI FQQLYVNRDI
     TKSEDVVRRA ERAGASAIWI TVDSPVVGKR EMDERFNLQV EARDDPSRKG QGVAKTMASF
     ISPFIDWDIL SWLRSLTKLP IVIKGIQCVE DAVQAYHCGV QGIVLSNHGG RSQDTAQAPL
     LTLLEIRRYA PFLLESKMQI FIDGGIRRGT DVLKAIALGA TAVGLGRPTL YSLAAGYGEQ
     GVRRAVEILR QEIESNMVFL GVTNLKELGP HLLNTARLER DVVGIGSFYS FILTRNDRVR
     LTVVARSNYD TVKENGIFLD SGNHGQHRFR PHNGNLAHVY MHTQKELTAL VIKSLDEISG
     SFDYVVCAHK AIDQEAVVTR LQPAINEKTT IVIIQNGVGN EEPFRNTFPM SSIITCVTWV
     GATQTSPGTV KHTKSEDMQI GLFPNASVDE TLERTRLNTF ASLLEEGRTK FQVLEDMQRQ
     RWEKVVWNAA WNPLTTLTLL DTQSWLHSST DATPLTRRLM REVIDVGRRC GVPLEYGLVD
     ELMDRINSLP GVGSSMQTDY KNGRPMEVDV ILGFPAKKSK EFAMTAEQPT PAPPHSAGHV
     IKPSAMHVEE IPGQPSKIQN GDTALALFEN FDELHEDVDP GELKRLVRKI DFMILPFLAV
     CYAFYYIDKT TLSYAAIFGI NEDLGLSGEQ YSWLSSVFYF GFLVWALPTN FLMQKFPVGK
     YLGANIFLWG FFLMLQAAAK NFVQLAVLRV ISGAAEACSD PAFMLITSMW YTRRQQPIRI
     GLWYTANGFG IALGGLLGYG IGHIKGALSS WKYEFLIIGA LCSLWGILIV IFLPDSPVTT
     RYLSPREKRL AVERLRENQT GVENKTLKPA QIYEAFLDWK VWVFLLLGLS GNIPNGGISN
     FGTLILKGFG FSTLVTTLMQ IPYGAFIALM ILFSIWLNDR LPQNNRCYVT ILFLLPNLVG
     SFGLCYLSES NKVGRLICYY LTGSYNASFV LILSILTANI AGHTKKVVTN AMIFIGVCAG
     NIAGPFFYKE AQAPRYPLGI WSMIVSHFVE ILLVIVLRTA LAWENRRRDR LQGIGSGGEG
     EEARQWEMDR TAFSDLTDKE NMNFRYVY
//
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