ID A0A0V1CD34_TRIBR Unreviewed; 1200 AA.
AC A0A0V1CD34;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN Name=POR {ECO:0000313|EMBL:KRY47241.1};
GN ORFNames=T03_8421 {ECO:0000313|EMBL:KRY47241.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47241.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY47241.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY47241.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:KRY47241.1}.
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DR EMBL; JYDI01000250; KRY47241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CD34; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 2.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR009581; FAM20_C.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF06702; Fam20C; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..413
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1200 AA; 137469 MW; 6520A500EC3A3F53 CRC64;
MDEQLGSGDA GSWLSFVDWL VLGFGLLVAL AYFWQNKFES RRSQISVSFK PIIPAQTSNG
TLDTHSFVAK MKAAGKNMVV FYGSQTGTAE DLAFRLAKDA VRYGMKAIAL DPEEYDPVFG
LGNKTYEHFN AMGKYTDKQL AKMGATRLCQ LGIGDDDGKH FNITNVGEDV SIREYELSII
EDCDTKGVFC GEVSRLGAYR NQKAYEAGDH LAVYPENDGE LVEQFGKLFN VDLDTIFTLT
NVDPLTYYVD ISTPPKTNVV KELSQYCSDE REKNFLLSMV TMEEKSRRKY SEWVIHDHRT
LLDILIELPS CRPPLDLLLE LLPRLQPRFY SISSSPKVDP SLVSITVIVL KYTTPIGRPG
KGVATNYLAS KIAVENKPHP QVFLLETDIS HLQDICLLNQ VPIYIRRSQF RLPHSPLTPV
VMIGPGTGIA PFRGFIQERA MLKQTGREVG PMILYFGCRK RKEDYLYGQE LEAWLKDGTL
SELHVAFSRD QPRKVYVQHL MLERKQSIWS LLQNGAFFYV CGDARNMARD VHSALMQIIA
GEGDMNADEA AAYFKQLESQ KRYQADVWRM RLNGRTSVSG RLVVLVPYGK AHVARYHQWM
QCDILRAQTG SEQLSLEDEY KMQKSWQEDE DKLTFIVVAK QLWQESRFDD VGAMVGDVNL
FFTPDQRSAE VEVMIAEPAW RGRGLGKEAV KMMLVYAFQQ LHVERFVAKI RSDNEPSLAL
FQSLQFEQFC RVDVFQELHM ELILHPDLVN VWKQDTNYAE IAYPCEQMND QMEQDDYEFL
LENHIALDRV GKTVGQSLLA QLRPRLRHNS SKAKIRSLLS LPWAVLLGQP DCSDEVTVYD
YLLEHFGNDI QNTTIWDRYY LSMSTCRMYN SETVVDQLLN LLVTMPIQDV KNMEAGTQLK
LLITFENNYS ALFKPMRQNR EEETNPNHFY FSDFERHNAE IAAYHLDRIL KFYKAIPTVG
RRINVTADIE LNSKLSPGLN DTFFLSPDMI EGSMQIFLPD EEMVPTDYVR SPFRRNKQLA
EWQYNKNFCN EKVVRLEPYN NGSRLLEMID AYIFDFLIGN QDRHHFEFFN LTNNGHLGFI
MNLDNGRGFG DSKKDDFDIL APLVQCCMIR PRTLKRLLDY YFGPVSLSTA LNRSMASDPL
APILADKHLL AIDRRLEAVL LQVSKCINDK EGHFDQVVRT TYSNDLPTVA AESVLVDIQS
//
