ID A0A0A3W2Z6_9GAMM Unreviewed; 330 AA.
AC A0A0A3W2Z6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GW12_24910 {ECO:0000313|EMBL:KGT46434.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT46434.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT46434.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT46434.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGT46434.1}.
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DR EMBL; JPQO01000206; KGT46434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A3W2Z6; -.
DR STRING; 1509403.GW12_24910; -.
DR PATRIC; fig|1509403.3.peg.2478; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG0633; Bacteria.
DR Proteomes; UP000032870; 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; cd06190; T4MO_e_transfer_like; 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: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; 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}.
FT DOMAIN 2..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 99..198
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 330 AA; 37100 MW; CE3D326DBDB2B128 CRC64;
MYKIQIEGQG EFHCAADDVL LRGGLRQGLG LPYECNAGGC GTCKIEVLSG EVDNLWAEAP
GLSDRDRRKG RLLACQCRPK SDCVIKVRLD EQCTPKILPK QQAVKLKHVQ PITHDILEIH
LQSDEPAKFI PGQYALLWVN EQLLRAYSMA NLPNDEGLWI FQIRRVPDGK MTNLLFDEQQ
RQNAVIQIDG PYGLAHLQEQ PRPIVCVAGG SGLAPMLAIA RGVAVNPQLQ HHKVWFFHGG
REQRDLLTEQ QLRDWTELGS RLNYVPATSS ELIEGIRSGF IHEVIDDVLG EQLIQHEIYC
AGPPPMVKSI EQMAHQAGIP QQQIHFDRFF
//
