ID A0A150GJZ8_GONPE Unreviewed; 581 AA.
AC A0A150GJZ8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=FAD synthase {ECO:0000256|ARBA:ARBA00012393};
DE EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
DE AltName: Full=FAD pyrophosphorylase {ECO:0000256|ARBA:ARBA00031145};
DE AltName: Full=FMN adenylyltransferase {ECO:0000256|ARBA:ARBA00031871};
GN ORFNames=GPECTOR_17g778 {ECO:0000313|EMBL:KXZ50142.1};
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:KXZ50142.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001332};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004726}.
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:KXZ50142.1}.
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DR EMBL; LSYV01000018; KXZ50142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GJZ8; -.
DR STRING; 33097.A0A150GJZ8; -.
DR OrthoDB; 5475801at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd00885; cinA; 1.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23293:SF9; FAD SYNTHASE; 1.
DR PANTHER; PTHR23293; FAD SYNTHETASE-RELATED FMN ADENYLYLTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF01507; PAPS_reduct; 2.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 328..495
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 61498 MW; 1B27818A68863079 CRC64;
MDILAHIDSI PDAVVAEKAR KAIQVLRRTC ALYPLDKIAF SFNGGKDSTV LLHLLRAAVA
QLQGPDTPGL GGILSFYFRK NDDFTEVKQF VEGADKQYSL DVEYIAEQDF KKGLCDYLES
TGVMAIVLGT RRGDPNAGGQ DTFCPSSEGW PPFMRVNPII DWTYHEVWVF LRAVRAPYCT
LYDHGYTSLG GTGNTLPNSS LRRPDGGYEP AYALADGRQE RSGRLHAAQP KSPAPLQHHN
HSQGGHVDKG SHATALDRLS SGGRGRGDGA VASGTAAAVA DGAGDGEEVP GADGEDGRAA
DRRPAGPRSG GGSPLPGPGG SELTKSAAIV IIGDELLSGK VEDVNARFLC RELRSLGWQV
LRVVFVPDDV DEIASAVRAL AAVVEVVITA GGIGPTLDDV TMQGVALAVG QPLVRLPDLV
SRLSEYFGGM DALTPAHLKM AEGPAAAELI DYTLPGADQP SKFPLVRVNN VYVLPGVPSL
LVQKWTALRP RLEAAALAPF RNATLKLSLK VDETTIAPAL ERVASAHGLD VAVGSYPVEQ
GIIITLDSKN TEALQAAIAD ITELLPGEAL VAMERDVDSL T
//
