ID A0A380TND9_9PAST Unreviewed; 339 AA.
AC A0A380TND9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=HCP oxidoreductase {ECO:0000313|EMBL:SUT87387.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:SUT87387.1};
GN Name=hcr {ECO:0000313|EMBL:SUT87387.1};
GN ORFNames=NCTC10801_00158 {ECO:0000313|EMBL:SUT87387.1};
OS [Actinobacillus] rossii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae.
OX NCBI_TaxID=123820 {ECO:0000313|EMBL:SUT87387.1, ECO:0000313|Proteomes:UP000254649};
RN [1] {ECO:0000313|EMBL:SUT87387.1, ECO:0000313|Proteomes:UP000254649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10801 {ECO:0000313|EMBL:SUT87387.1,
RC ECO:0000313|Proteomes:UP000254649};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UFRQ01000003; SUT87387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380TND9; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000254649; 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:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06215; FNR_iron_sulfur_binding_1; 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; 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 PRINTS; PR00406; CYTB5RDTASE.
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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000313|EMBL:SUT87387.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 9..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 252..339
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 339 AA; 37067 MW; FA55DC11765DD819 CRC64;
MANTNKNPLC INELQVHSII KEAPNVTTLN FIAQDFYQYK AGQYAMVSIR NTPHIARAYS
LSSTPGESRF VSITVREIEN GKGSTWLNNE VKVGDQVWFS DPMGDFSCEK VIAENYLLAG
AGSGVTPVIS MARWLLVNRP EVNVTVIHSV HSPEDVIFKS EWAELVAKYP KLNLVINASV
NATDEMKSGR INKEMVAAAV PNIQDYTVMT CGPESYMNAL KTIVLELGVP EERFFTEAFF
DSATQGGVDY DKQTTLTING ATKQTFNVPV GMTLLAALEE NQQPVTSGCR TGLCGLCKTQ
VTSGDIEVVR TGDLTETEIA QGYVLACSCR VKKDVNITA
//
