ID A0A151NSH7_ALLMI Unreviewed; 2790 AA.
AC A0A151NSH7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN Name=PRRC2C {ECO:0000313|EMBL:KYO39796.1};
GN ORFNames=Y1Q_0006681 {ECO:0000313|EMBL:KYO39796.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO39796.1};
RN [1] {ECO:0000313|EMBL:KYO39796.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO39796.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-
CC dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+);
CC Xref=Rhea:RHEA:54860, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16980, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:138375;
CC Evidence={ECO:0000256|ARBA:ARBA00023916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54861;
CC Evidence={ECO:0000256|ARBA:ARBA00023916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octan-3-one = H2O + NADP(+) + pentyl
CC propanoate; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:80946, ChEBI:CHEBI:87373;
CC Evidence={ECO:0000256|ARBA:ARBA00001029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54841;
CC Evidence={ECO:0000256|ARBA:ARBA00001029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octan-3-one = ethyl hexanoate + H2O +
CC NADP(+); Xref=Rhea:RHEA:54856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:80946, ChEBI:CHEBI:86055;
CC Evidence={ECO:0000256|ARBA:ARBA00001105};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54857;
CC Evidence={ECO:0000256|ARBA:ARBA00001105};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + sulcatone = 4-methylpent-3-en-1-yl acetate
CC + H2O + NADP(+); Xref=Rhea:RHEA:54864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16310,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138373;
CC Evidence={ECO:0000256|ARBA:ARBA00000299};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54865;
CC Evidence={ECO:0000256|ARBA:ARBA00000299};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000458};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11261;
CC Evidence={ECO:0000256|ARBA:ARBA00000458};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptan-2-one + NADPH + O2 = H2O + NADP(+) + pentyl
CC acetate; Xref=Rhea:RHEA:54836, ChEBI:CHEBI:5672, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87362;
CC Evidence={ECO:0000256|ARBA:ARBA00000019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54837;
CC Evidence={ECO:0000256|ARBA:ARBA00000019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptan-4-one + NADPH + O2 = H2O + NADP(+) + propyl
CC butanoate; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:89484, ChEBI:CHEBI:89719;
CC Evidence={ECO:0000256|ARBA:ARBA00001839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54853;
CC Evidence={ECO:0000256|ARBA:ARBA00001839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexan-3-one + NADPH + O2 = H2O + NADP(+) + propyl
CC propanoate; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:89828, ChEBI:CHEBI:89891;
CC Evidence={ECO:0000256|ARBA:ARBA00000279};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54849;
CC Evidence={ECO:0000256|ARBA:ARBA00000279};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexan-3-one + NADPH + O2 = ethyl butanoate + H2O +
CC NADP(+); Xref=Rhea:RHEA:54844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88764, ChEBI:CHEBI:89891;
CC Evidence={ECO:0000256|ARBA:ARBA00000531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54845;
CC Evidence={ECO:0000256|ARBA:ARBA00000531};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU361177};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004524}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|RuleBase:RU361177}.
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:KYO39796.1}.
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DR EMBL; AKHW03002184; KYO39796.1; -; Genomic_DNA.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR009738; BAT2_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002257; Flavin_mOase_5.
DR InterPro; IPR033184; PRRC2.
DR PANTHER; PTHR14038; BAT2 HLA-B-ASSOCIATED TRANSCRIPT 2; 1.
DR PANTHER; PTHR14038:SF6; PROTEIN PRRC2C; 1.
DR Pfam; PF07001; BAT2_N; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01125; FMOXYGENASE5.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Monooxygenase {ECO:0000256|RuleBase:RU361177};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525}.
FT DOMAIN 618..762
FT /note="BAT2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07001"
FT REGION 614..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2638..2674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2718..2790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..716
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2111..2125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..2171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2172..2319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2648..2674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2790 AA; 307497 MW; C7DEAC427E310AF7 CRC64;
MVQRVAIIGA GVSGLASIKC CLDEGLKPTC FERSNDIGGL WRFSETTKSG RISVYRSVIT
NTSKEMSCFS DFPFPDNFPN YLHHSRLLNY FRMYAEHFDL LKYIHFGTTV HSIRKCPDFS
ASGQWEIVTE ANGEQKSSIF DAVMVCSGHY AEPHLPLDSF PGIRNRFKGQ CLHSWEYKDS
DDFKGKRILV VGTGNSGGDI AVDLSHVAAQ VFLSTRSGTW VVSRVSNQGF PLDMVFTTRF
ANCVEWLLPS VLASRIKREK FSAWFNHENY SLFQQKSQEL HLIVNDELPS CILCGAVVVK
PNVKEFTETS AIFEDETVMD NIDVVVFATG FTVSFPFLEE SVQNVCKSKT SLYKYVFPPQ
LEKPTLAVLG FIQLTGSIMV GTELQARWVT RVFKGSNKLP QVSRMMTDVS KEKELLMKRG
FSRDYNNTRA SFVVYMDEIA SCIGVKPNVL LLFLTDPKLA LEVFFGPCTP YQYRLVGPGK
WGGARNAILT QWQRVLTPLR TRVVNDSPNQ SSALGWFTLL ASEFCGNTWH GMAQGTEVVC
NQEIRTTSRN MQNRAQVTGN SKRVTHSMGS DQLPIQMSID IQEQAGAAAP DAAARLVFYV
CARGTRLDEF PSKCRKRQGK SLETQKTTVA TRHGLQSLGK VAISRRMPPP ANLPSLKAEN
KGNDPNVNIV PKDGTGWASS KQEQHEEEKP PEVPPTQPKP APPPPPPPPP PEAPPVAKSW
ASTKPGGQGD GPALPVNRYF QQEFPSLQAA GDPEKSGKEK DAAEEPQGPG PNSRPQNQEV
KTPGQEDGSA AGAAEQTDAQ KAAEKRDVRM PQVPQPKLNG QQQPGISSQY RAMMPPYMFN
QHPRMAYPPM QGPSRFPASS EPSRGPRGRG PPSRCAEPVE RPSILSASEL KELDKFDNLD
AEADEGWAGA QSEVDYTEQL NFSDDEEQGS SQKEKESGDE QMPSKDSQSI DSHKEAEEQS
SSKSSTQATS PGVKGPCGKS TQPDQERGPA PLQPSVHERG SSTLPPKSIL QQHPPPDRQA
GPGRQGPFPP KPVPDEDEIW KQRRRQQTEV SAAVERARKR REEEERRMEE QRKAACAEKL
KRNNNEEKES PPVFTRQDSG RNEKESLQVA HDSDLDTGAQ PRPAVSSGYS KQFQKSLPPR
FQRQQAMQPH PQHLASMGFD PRWLMMQSYM DPRMMSGRPA MDVPPMHPGI MPPKPLMRRD
QMEGSGTSSD SFEHIVRSAR EHAVSLSEPR MMWGSDPYPH AEPQQPSTPP KVLEEPEDLR
PEACLEQERI AVTTAYPVEH NQLDSHPKAD FFREPGEVDV QKFPSRSLED IQPLQTDAPS
SALSFEVVDE NIAHSSQEEL VPIGESHSAL KKSIYHGSSH SLKPEEQRNE TSSGIPKVNS
RPVETKEPVE RPEIKPKKEG FMSNRISEGP KTEKPFKPKS ETRWGPRPSY GRREEGSDRP
IRRSGPIKKP VLRDMKEERE QREEREQRKE KEGEKVANEK FGKSDKTEKK EQPQLPPPQA
EPEKSTSGSA PVAKKVPQDT VQVSETEDGN LAESTVKPAV QPLPVVQQSL PVVQSPPVQQ
PPPVVQQPAV QQPITQQPPP AVQQPSVQQP VSTVKEDKQS EKPVSKEVVE KPRLETRPVK
REPGLPPRTY WKEARDRDWF PEQGYRGRGR GEYYSRGRSY RGSYGGRGRG SRGHNRDYPH
YRDTKPRVDH VPPGPVRQRE ESETRSESSD FEIIPKRRRQ RGSETDSDSE VHESASDTLL
SDKDSLSKGK QPKREERVEG KKPPKPLSFK PENHVRIDNR SLEKTYIRED ENKPKPGFLP
KGEPSRRGRG GMFRRGDQAN EEWETASESS DFNERRERDE KKMADVTTQR PGIDRQNRRG
NNGPAKSGRN FSGPRSERRS GPPSRSGKRG PFEEQTASMT TVEPTSSNSL HQEEGSGGAV
VQKNSKDVCG KKRDDSKPGP KKPKEKVDAL SQFDLNNYAS VVIIDDHPEV TVVEDSQCNL
NDDGFTEVVS KKQQKRLQDE ERRKKEEQTV QVWTKKSSSE KGRELWENKV APTTVITDIS
KKLGPISPPQ PPSVSAWNKP LTSFGSTTSP EGAKPGQESG VELGIETIQF GAPASSGSDN
EVGPVLSEKP TDKLPEPKEQ RQKQPRAGPI KVQKLPDLSP VENKEYKPGP IGKERSLKNK
KVKDAQHGES DGQEKPSPTA VRSPEPVTTK ETKAVNELST EIGTMISVST PEFGTNTKME
SARKAWENSP NVGEKSSPVT SAASPITGSN SGSSSSSSGP SSGSYSSFSS ASMPPIPVAS
VTPTTSLSGA GTYTTSSLST KTTTTSDPPN ICKVKPQQLQ TSSLPSASHF SQLSCMPSLI
AQQQQSPQVY VSQSAAAQIP AFYMDTSHLF NTQHARLAPP SLAQQQGFQP GLSQPASVQQ
IPIPIYAPLQ GQHQAQLSLG AAPAVSQAQE LFNSSLQPYR SQQAFMQSGL SQPSPVVLSG
TALHNFQTVQ HQELAKAQSS LAFQQTSNTQ PIPILYEHQL GQASGLGGSQ LIDTHILQAR
ATLTQASNLY SGQVQQPGQS NFYNTAQSPN ALQQVTVPLP GSQLSLPNFG STGQPLIALP
QSLQPPLQHT PPQAPAQNLS RPAQVSQPFR GLIPAGTQHS MIAATGKMSE MDLKAFGSSI
DVKPGTPPVT GRSTTPTSSP FRASSTSPNN QSNKMNSIVY QKQFQSAAAA VRMTQPFPPQ
FAPQAKQRAE VLQSTQRFFS EQQQPSKPIG GKVQKVDENG SKPTEAMADS SGVCQEKVEE
KPTPAPTATT KPVRTGPIKP QAIKTEETKS
//
