ID Q2UQP5_ASPOR Unreviewed; 684 AA.
AC Q2UQP5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 03-MAY-2023, entry version 110.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE56120.1};
GN ORFNames=AO090005001159 {ECO:0000313|EMBL:BAE56120.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE56120.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE56120.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AP007151; BAE56120.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UQP5; -.
DR STRING; 510516.Q2UQP5; -.
DR EnsemblFungi; BAE56120; BAE56120; AO090005001159.
DR HOGENOM; CLU_000395_3_3_1; -.
DR OMA; MYYDSMI; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT DOMAIN 3..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 602..682
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 548..582
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 684 AA; 75281 MW; 6660ECEF410B1CA5 CRC64;
MESLKTLLVA NRGEIAVRIL KTAKKLNLRT IALYTEPDAA SAHVQLADEA FLLDGPPSKA
YIDGDQIIKL AKRNHVDAII PGYGFLSENA DFARAIAKAG MVFAGPSPEC IEAFGLKHTA
RDLATKAGVP IVPGSTGLVT SEEDAVKVAK DLGFPVMLKA TAGGGGMGLL TCSSEDEVRE
SFATVRSRGE ALFKNAGLFI ERYYPSSHHI EVQVFGNGDG KAIAIGEREC SIQRRHQKII
EECPSPFVTR NPGLRESLGD AAVRLAESIK YGSAGTIEYL VDDETGAFFF LEMNTRLQVE
HGITELCYGV DLVELMLKQA DAQLSGKKGL EVAFLTGITV DAPSGAAIEA RVYAENPTKD
FAPCPGTLQS VEWKELPGSR IDTWVYRGIK VSANYDPLLA KVMLHSPSRT QAIEGMRTIL
TQSRICGPPT NLEFLAEILT DERFVTGNTL TRFLDDFQWK LVTALKKVLN EGNGDITFSN
KLISMIGCGN CVDILGSKKG YTPDRPWLFE EFDQITFYRV SEEEYEKELA LFNSGRYEYQ
WEEVIFDMAE HNKLLHDTKE EVAAIRARQR KAQDEMDKLE AELLEHWAKE KAEKGVPVDA
IENLLKDPQI LPIEAPLNAN IWKVEVKQGD KLDEGQIVVI LEAMKLEIAV RTELHAAGAT
VEKVLVQPGD SIEAGKPLIL VRNA
//