ID A0A150H1I6_GONPE Unreviewed; 896 AA.
AC A0A150H1I6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aminoglycoside phosphotransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GPECTOR_2g1278 {ECO:0000313|EMBL:KXZ55728.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ55728.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KXZ55728.1}.
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DR EMBL; LSYV01000003; KXZ55728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150H1I6; -.
DR STRING; 33097.A0A150H1I6; -.
DR OrthoDB; 276350at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT DOMAIN 48..298
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 619..722
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 734..882
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 896 AA; 93556 MW; 5F8E130459C591D0 CRC64;
MTSKSFSTLQ SLGPVRTGHQ FDVAGLQAYL QTQLPELFQG AGASHIVVQQ FQHGQSNPTF
MISLPWSGQR LVLRKKPPGK LLASAHAVER EYAVLAALSP VGFPVPRPVH LCTGGVPLGT
PFYLMECAEG RVFLDPNLPE LQPQQRSEVY AHMAQTLARL HTLKPSALGL SSYGSPAAYC
ARQLRRWTSQ YAASVPAPDP SVSRLTAWLA AHVPAEDAAP PRPALVHGDY RLDNIVFGTR
GSAPAGGGGG GGGGLVPLAV LDWELSTIGN PWADVAYNCL PYHMPPGLLV LQRLTRDPRA
GTPSGLPPGI PTEAEYLAAY CAAAGVAAPP PAEWAFYVAL SLFRCLAILA GVAARSRQGN
ASSANAAAVA SEEVLAALTA AALGVIERAE AEAAAGGQTG KGGAAGGCKC SNPACTCGVD
GGRTAGGKCS CSGCGGAAQV KQQQQETQQV PACDAAGGDG LLGLSPRAAE LRSRLAAFMA
DHVYPAEEVL EAHAMGPQET RWTIHPLMEE LKAKAQQAGL WNLWLPASLA SRLGWLAEAA
RAGAGGADPR VAPVLLGAGL SHLEYAHLCE LMGRSAWAPE VFNCSAPDTG NMEVLAKYGS
REQQLAWLLP LLAGSIRSCF AMTEKAVASS DATNITATIA RSACGQRLTV SGVKWWTSGA
MDPRCKIAIF MGKTDPRAAT HKQQSMVLVP MDAPGVKVVR PMLVFGFDDA PHGHAEVHFT
DVTVPASNLI LGEGRGFEIA QGRLGPGRLH HCMRLVGAGE RAIELMAVRA AQRVVFGKPL
AQQGAFQAKL GRCRIAVDSS RLLVLAASDA LDRLGFKGAA GAIAAAKVAT PSAVLEVLDA
AIQAHGGAGV SQDFVLARLW TAARTLRIAD GPDEVHLGTL AKLEMKRLGP GKVSKL
//
