ID A0A100I974_ASPNG Unreviewed; 1213 AA.
AC A0A100I974;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Unnamed protein product {ECO:0000313|EMBL:GAQ36992.1};
GN ORFNames=ABL_01966 {ECO:0000313|EMBL:GAQ36992.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36992.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992}.
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:GAQ36992.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BCMY01000002; GAQ36992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100I974; -.
DR PaxDb; 5061-CADANGAP00002553; -.
DR VEuPathDB; FungiDB:An02g11040; -.
DR VEuPathDB; FungiDB:An18g00040; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1175291; -.
DR VEuPathDB; FungiDB:ATCC64974_53840; -.
DR VEuPathDB; FungiDB:M747DRAFT_313165; -.
DR OMA; LATANHW; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003994; F:aconitate hydratase activity; 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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF2; HOMOCITRATE DEHYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..465
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 1213 AA; 131462 MW; E7182B5E878A7010 CRC64;
MVGLTLPVVG TQLQVALVLL IVAPSFILFG YNQAVLGSLL SLQSWVSVFP AIDTINTSGA
QRSHNSTSQG ACNASFQMGC LIGALSLSLY GDKLGRRKTV FIGAVITVVG QALQVSATTL
IQLVVGRVVL GFAIGQISGT VPVWLSECAS PKYRGQLGIC TGIFISTGYT LCNWIDLGFS
YLPSTTGQWR APLAIPFLFS AMILVSAFTF PESPRWLISR GRVEEATDSL CRYRGKDAHD
EMIMGEIAHI QLALEGSGTM SILDIFDRKD KTRLLLRFWL CMGLNFFQQA CGGNLISVYS
STIFENYLHM TPTMSRVLAS CVLSWKTLCC IITFWTIDNW GRRLSFMVSG AGMSVCMAVL
AVTTGLGKIT HPMAIAYVAF MFVFNFFYPI GFMGGNFLYT AEIAPVRLRA AMSSLATANH
WLWNLVVVLV TPVAIDTIGC WYYVIYALIS ATIPVCVYFF YPETMHRSLE MLDRVFVDAP
SIWKIVPMAR GLPLGEVGTA ESGVLYSHLD TTFDERIERG KTQLKLRPQR IACQDATAQM
ALIQFMSAGL DTAAVPTTVH CDHLIVSRDG ETQDLARALD NHKEVYDFLE SACQKYNMGF
WKPGAGIIHQ IVLENYAFPS GMMIGTDSHT PNAGGLGMIA IGVGGADAVD VMAGLPLELQ
APKVLGVRLT GQLSGWASPK DIINAVAGTL SVKGGTGSII EYFGPGAQTL SATGMATVCN
MGAETGATTS IFPYAPQMAD YLRANHRREM ADAVKSIAPE LQADQGAEYD NVIELDLSTL
EPRINGPFTP DFSTPVSRFG EAAAENQWPG ELTAALIGSC TNSSFEDMGR AASLAQQALD
AGLEPKMPLL VSPGSVQTRE TLKDAGILPV FERLGATMLP NACGPCCGSW DRVDMPKGTP
NSIITSYNRN FSGRLDSNPA TNVFLASPEL VIAKAFSRDL SFDPTTDTLP TPTGEQFHFL
PPTSDSLPSK GYLSSDSAYA PPPANRDNIS VKIDPSSLRL QKLSPFPPWP GHDFENCAIL
IKTAGKCTTD HITPAGPWFR YRGHLENISN NTLIGATNAE NGKVNSIRNQ LTKQDGQEVP
ATARHYKENG VPWVVIADHN YGEGSSREHA ALQPRYLGGV AIIAKSFARI HEANLKKQGL
LALTFENEQD YDRIRAEDRI SIMGLGEGEF VPGSTLRLVV NGGEWEAVLR HSFTEEQIGY
FRSGSALNLM AGK
//