ID A0A067KMY2_JATCU Unreviewed; 533 AA.
AC A0A067KMY2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=JCGZ_09768 {ECO:0000313|EMBL:KDP36348.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP36348.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP36348.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP36348.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK914441; KDP36348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067KMY2; -.
DR STRING; 180498.A0A067KMY2; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR32448:SF25; BERBERINE BRIDGE ENZYME-LIKE 8; 1.
DR PANTHER; PTHR32448; OS08G0158400 PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..533
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001643028"
FT DOMAIN 74..248
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 533 AA; 59874 MW; 8B0A7209D5A467FE CRC64;
MTSLLLSSFL LFLSLCIIST SASSSPDGET IIECLLTHSQ SSNPISNAIY TPKNTSYSSV
LQTYIRNLRF NESTTRKPLL IVTALHESHV QASIICARKH GLQMKIRSGG HDYEGISYVS
IVPFFILDMF NLRKIEVDVV SETAWVEAGA TLGEVYYNIG NKSNIHGFPA GVCPTVGVGG
HFGGGGYGNM MRKYGLSVDN IIDAKLIDVN GRLLDRKSMG EDLFWAITGG GGASYGVVIA
YKIKIVRVPE IVTVFRVQRT QEQNVTDIVY QWQQIAPKID DDLFLRVTFD VINSTQGSGK
TIRATLRALF LGDSTKLLSI INAKLPQLGL IQSECIEMSW LESVLFWTDF SLGTPTTALL
SRTPQVLTHL KRKSDYVQEP IPRNGLESIW KKMIELQVPQ LTFNPYGGKM AEIPADAKPF
PHRAGNLWKI QYATNWNEDG TEAANRYINL TRQLYNFMTP FVSKNPRAAF LNYRDLDLGI
NHNGKRSYLE GRVYGIKYFK DNFNRLVKIK TKVDPGNFFR NEQSIPTFPY WKN
//
