ID A0A163JES8_ABSGL Unreviewed; 724 AA.
AC A0A163JES8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:SAL98852.1};
GN Name=ABSGL_04417.1 scaffold 5409 {ECO:0000313|EMBL:SAL98852.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98852.1};
RN [1] {ECO:0000313|EMBL:SAL98852.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98852.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; LT552359; SAL98852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JES8; -.
DR STRING; 4829.A0A163JES8; -.
DR InParanoid; A0A163JES8; -.
DR OMA; IYYDPML; -.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
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 FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 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; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866:SF127; -; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 8..462
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 724 AA; 80164 MW; 7AA30AACDA188C04 CRC64;
MVATLNTPIH KVLIANRGEI ACRVIRTCRR LGIATVAVYS DSDENAPFVK LADEAYHIGP
SVAAESYLVG AKLIDIAKRS GADALHPGYG FLSENADFAD QVVAAGINFI GPTADSIRAI
GDKIAAKVFI KNHASSIPLI PGYNGEDQSV ERLEQEAKRI EFPVLLKASA GGGGKGMRAV
YETSKLRDEI EAAKGESLRS FGSDKLLIEK YFTSIRHVEI QIFGDKYGNV YHINERDCSI
QRRHQKVVEE TPSPAVDDAL RQAMTSAAVE LGRKLGYLGA GTAEFILDEK TRRFFFLELN
TRLQVEHPIT EAISGLDLVE LQLLVAQGAN LKELGLLDNI PFQGHAIEVR LCAEDPDNDF
GPRTGVIQKW SPGNAAKDLP GVRYDTGIED GSEISVYYDS MVAKVIVHAP TRAEAVRRMI
MALSRTVILG VTTNQKFLIS IMNNPRFQSG TFDTNFITLE NDRLFQKTTT ALVQSSVVAA
TLFDWCVRKN QQVHLRNMAP NWRNVPWRNP SVRYLINQEQ EVSITYAYQG NEQRDHRHAF
QCGVALAPEE APKSKEDPKK IAQGPELSLS AVLYDTDFGK ETPGPKGVQG AKGLLRATID
GCQQYFYICE QIHDVNEKSI FVHDFVQGHQ IELFKIDRLK SAAAAGEDDR VTPYTSSMPC
RVLKVLAPTG TIVKKNDPLL SIESMKTEVK LLSRHEGVVT MRVEENQLVD ARVLLCQVDE
IKKE
//
