ID I4Z540_9BURK Unreviewed; 346 AA.
AC I4Z540;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=2-polyprenylphenol hydroxylase-like oxidoreductase {ECO:0000313|EMBL:EIM31332.1};
GN ORFNames=LepocDRAFT_00000590 {ECO:0000313|EMBL:EIM31332.1};
OS Leptothrix ochracea L12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=735332 {ECO:0000313|EMBL:EIM31332.1, ECO:0000313|Proteomes:UP000053899};
RN [1] {ECO:0000313|EMBL:EIM31332.1, ECO:0000313|Proteomes:UP000053899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EIM31332.1,
RC ECO:0000313|Proteomes:UP000053899};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stepanauskas R., Masland D.,
RA Poulton N., Emerson D., Fleming E., Woyke T.;
RT "Improved High-Quality Draft sequence of Leptothrix ochracea L12.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; JH660693; EIM31332.1; -; Genomic_DNA.
DR RefSeq; WP_009453611.1; NZ_JH660693.1.
DR AlphaFoldDB; I4Z540; -.
DR HOGENOM; CLU_003827_7_0_4; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000053899; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06189; flavin_oxioreductase; 1.
DR Gene3D; 3.10.20.30; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000053899}.
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..201
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 346 AA; 37193 MW; E60B4240BBE26703 CRC64;
MTCSVTVQPS GRHFEAQPDE TLLAAAIRQG VGLPYGCKDG ACGSCKCQLI SGTVVHGAHQ
AKALTPEEEA AGKILSCRAV PQTDCVLDAP QVTAVDQFPV LKMPARVISI SKLTRDVAVV
QLQLPANQTF RYQAGQYVDV LLRDGARRSY SMASAPRDGQ ISIELHIRHL PGGKFTDHVF
GAMKEKEILR LEGPFGSFGV QAGEAPIILL ASGTGFAPIK AILEVLQAEA ATRPVSLYWG
CRTKADLYAE DWIKQALTTL PQLRYVPVLS EPRTEEAWAG RTGLVHEAVM QDHPNLAEHQ
VYACGVPVMV DAAQRDFVAQ CALPAQAFFA DAFTSEADKA AVNAAE
//
