ID A0A168NSD0_ABSGL Unreviewed; 745 AA.
AC A0A168NSD0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Name=ABSGL_06844.1 scaffold 8678 {ECO:0000313|EMBL:SAM01107.1};
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:SAM01107.1};
RN [1] {ECO:0000313|EMBL:SAM01107.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM01107.1};
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 -!- 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}.
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DR EMBL; LT553503; SAM01107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168NSD0; -.
DR STRING; 4829.A0A168NSD0; -.
DR InParanoid; A0A168NSD0; -.
DR OrthoDB; 1381373at2759; -.
DR Proteomes; UP000078561; 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; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; PF01507; PAPS_reduct; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 68..225
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 745 AA; 84387 MW; CF9DE25F1B1BAF0F CRC64;
MHSTLVKNHG CTSRSTDPLL NGAEQFDTAY IEKTVYELAS MDDSLGHAVK EALTVIEQAY
KLYGMEAISL SFNGGKDCTV LLHLVVAVLS KLGYNRNELL RTVFVTYPNP FPHVDAFVHV
CAKRYNLNCV SIPGPMRQAL QQYLDTTQPR PKAIFVGIRR NDPYAERLTH FDMTDDGWPE
FMRVHPIVDW TYKDIWDFLI KLGIPYCSLY DEGYTSLGSM ENTHPNPDLE QQKGEYKPAF
MLKNELHERC GRFGSSKSDT SPHGSLTLGP ASHQSKVFVG QDHTSFDLKA LDATACKNVD
VAWLASDRQF WDGWSTKAMF LQQDGNFTTT NVLTTEGVSL CVVVLLGPSP ATSVIRAENH
LGPADSIAIE AIGNTTIIPI ELQQHRKQTN AYFASVHFSQ PDSYILKGRV EYRSYFWEQP
IYHSYRPTTF KSVNMAMVQP LYKLAQPSCN ARNPDHLEGN WMNKTAFQTA YPLDFYGMFG
PVQEDHAEFD RLFVPHQCRM EYISYGQATR CLEDKTIHVW ADANLRRNLK AFESANRWCN
ENKTAECVCN DDNEDPKHTI YPWAVDPLTP LVINKTWHGN TEIYYNPVDS IATKDWKKTI
KTQAAKLSAK PADIVILGFG NGDLPLTRVS PKDFAFAFEE LLQYVITEVY PHQTIVVRSP
QYFCCGTFGS TSWNIGRSAA FARVVRHIVN QQATDRVLLW DVYKLGIEEN TCVVDGSTYS
RKNVVNVENI LLWNLICPSR KSSPA
//
