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Database: UniProt
Entry: A0A100I974_ASPNG
LinkDB: A0A100I974_ASPNG
Original site: A0A100I974_ASPNG 
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}.
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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
//
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