ID A0A077M3L4_9MICO Unreviewed; 365 AA.
AC A0A077M3L4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Stearoyl-CoA 9-desaturase electron transfer partner {ECO:0000313|EMBL:CCH80411.1};
GN ORFNames=BN12_910018 {ECO:0000313|EMBL:CCH80411.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH80411.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH80411.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH80411.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:CCH80411.1}.
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DR EMBL; CAJB01000427; CCH80411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077M3L4; -.
DR STRING; 1194083.BN12_910018; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000035721; 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; cd06216; FNR_iron_sulfur_binding_2; 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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
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:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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; 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:UP000035721}.
FT DOMAIN 46..149
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 365 AA; 38901 MW; 2FB17697500921BF CRC64;
MSTQTRPTAS PWLARFRTGI AGVAESLATP LVPADYLDLV SPLRAGADLR GRIVAITPET
PDAATVTIRP GRGWLGHRPG QYIRIGVDVD GVRNWRAYSL THGPDQPAGT ISITVKAIEN
GVVSNHLVRR TRPGTLVMLD QATGEFCLPE RLPGKVLFVT AGSGITPVMG MLRHHLDDLE
DVVLVHSAPT ASDVVFGRRL RAYAASGRLT LHERATDEVG MLDLAELDSL VPDWREREAW
TCGPTGLLDA AEAHWEAEGL ADRHHVERFR PTVIEPGEGG TVTFAASGKV VEADGATPIL
DAGEDAGVLL PSGCRMGICF GCVSTLRQGA VRDLRNGEIT VAEPGDDLPV QTCVNAAAGP
CEIDR
//