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Database: UniProt
Entry: A0A1H1LLY0_9ACTN
LinkDB: A0A1H1LLY0_9ACTN
Original site: A0A1H1LLY0_9ACTN 
ID   A0A1H1LLY0_9ACTN        Unreviewed;       442 AA.
AC   A0A1H1LLY0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Predicted ferric reductase {ECO:0000313|EMBL:SDR75574.1};
GN   ORFNames=SAMN04489717_0415 {ECO:0000313|EMBL:SDR75574.1};
OS   Actinopolymorpha singaporensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Actinopolymorphaceae; Actinopolymorpha.
OX   NCBI_TaxID=117157 {ECO:0000313|EMBL:SDR75574.1, ECO:0000313|Proteomes:UP000198983};
RN   [1] {ECO:0000313|EMBL:SDR75574.1, ECO:0000313|Proteomes:UP000198983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22024 {ECO:0000313|EMBL:SDR75574.1,
RC   ECO:0000313|Proteomes:UP000198983};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; LT629732; SDR75574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1LLY0; -.
DR   STRING; 117157.SAMN04489717_0415; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000198983; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06198; FNR_like_3; 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; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198983};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..315
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   442 AA;  48919 MW;  AB24862B7B7F607A CRC64;
     MRALIVRHSP WLVWAGVAVG AGGLTLLWWT STLPPTSFGA QLTEAGRLTG LFAGYLVVIL
     LVLMARLPLL ERQVGTDRLA RIHSMVGRYV VCVTVAHMVL IWLGYALTAH ASLGAEVTDL
     LTGYPYVLWA VIGAGLFVLV GTVSATAIRS RVRYETWYLL HLLTYAGIAL AFWHQILTGA
     QFVPNAVARW GWIGAYAAAT ALLVWYRLLV PIRNLWRHRL EVAAVRTEAP GVVSVYLTGA
     RLDELGAEAG QFLRLRFLTR NAWWQSHPYS LSAAPNPSWL RVTIKALGDH TEQLQRIRVG
     TRVLAEGPYG ALTARRRSRH GVVLIAGGVG VTPLRALFES LPAEEGRLTL IYRASRHEDV
     VFRHELDEIA ADRRAVVHYL VGPPGPGQEP ALHPNWLRRL VPDVAERDAY LCGPGGMMTT
     AMESLRECGV PARRIHHEDF NF
//
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