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
//