ID C5T092_ACIDE Unreviewed; 444 AA.
AC C5T092;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Ferric reductase domain protein transmembrane component domain {ECO:0000313|EMBL:EER62045.1};
GN ORFNames=AcdelDRAFT_0322 {ECO:0000313|EMBL:EER62045.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER62045.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER62045.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER62045.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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}.
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:EER62045.1}.
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DR EMBL; ACQT01000004; EER62045.1; -; Genomic_DNA.
DR RefSeq; WP_005792968.1; NZ_ACQT01000004.1.
DR AlphaFoldDB; C5T092; -.
DR PATRIC; fig|573060.9.peg.4831; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000003856; Unassembled WGS sequence.
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; 1.20.120.1770; -; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-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; PF01794; Ferric_reduct; 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 Reference proteome {ECO:0000313|Proteomes:UP000003856};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..320
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 444 AA; 49548 MW; 68859B4DC02D24AB CRC64;
MKRIKVSLIA ILVLLTSLWL AADTLLPEPF NYFSFRSVFI QFSGVLSIGL MSIAMLLALR
SKWLDRHLNG LDKMYRLHKW LGICALVAAV LHWWLAKGTK WMVGWGWLER PARKPNAGET
LGAIEGWLRG QRGLAESIGE WMFYVAAVLI VLALIRRFPY HLFVKTHKWL AAAYLALAYH
SAVLTKFDYW TQPIGWLLAA LMLGGSIAAV LALFGQIGAG SKVQGTIESL TEYPALRVLE
TTVMLNDGWP GHAAGQFAFV TSDKNEGPHP YTIASAWNRS NPRLTFITKA LGDHTSHLRE
RLKIDLPVTV EGPYGCFDFE DTQPHQIWIG AGIGITPFVA RLKHRAANPD TRTIDLFHPS
ADFEQAAIDR LTADAAAAGV RLHLLVDGKD GRLNGERIRT AVPHWRSASV WFCGPAGFGQ
ALRDDFCANG LPDERFHQEL FEMR
//