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Database: UniProt
Entry: N8NZ90_9GAMM
LinkDB: N8NZ90_9GAMM
Original site: N8NZ90_9GAMM 
ID   N8NZ90_9GAMM            Unreviewed;       338 AA.
AC   N8NZ90;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Benzoate 1,2-dioxygenase electron transfer component {ECO:0000313|EMBL:ENU19706.1};
GN   ORFNames=F994_02566 {ECO:0000313|EMBL:ENU19706.1};
OS   Acinetobacter bohemicus ANC 3994.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217715 {ECO:0000313|EMBL:ENU19706.1, ECO:0000313|Proteomes:UP000013086};
RN   [1] {ECO:0000313|EMBL:ENU19706.1, ECO:0000313|Proteomes:UP000013086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3994 {ECO:0000313|EMBL:ENU19706.1,
RC   ECO:0000313|Proteomes:UP000013086};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. ANC 3994.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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:ENU19706.1}.
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DR   EMBL; APOH01000015; ENU19706.1; -; Genomic_DNA.
DR   RefSeq; WP_004649110.1; NZ_KB849164.1.
DR   AlphaFoldDB; N8NZ90; -.
DR   PATRIC; fig|1217715.3.peg.2509; -.
DR   eggNOG; COG0543; Bacteria.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_003827_7_0_6; -.
DR   OrthoDB; 9806195at2; -.
DR   Proteomes; UP000013086; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06209; BenDO_FAD_NAD; 1.
DR   CDD; cd00207; fer2; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR047683; BenC-like_FAD_NAD-bd.
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   NCBIfam; NF040810; BenC; 1.
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; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Dioxygenase {ECO:0000313|EMBL:ENU19706.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Oxidoreductase {ECO:0000313|EMBL:ENU19706.1}.
FT   DOMAIN          4..99
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          31..63
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          106..207
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   338 AA;  37354 MW;  DF331B5D3A67CBF3 CRC64;
     MSNLNVALQF EDGVTRFISV VQGETLSDAA YRQKINIPLD CRDGACGTCR AFCESGSFDM
     PEETYIEDAL TPEEAAEGYV LACQCRPTSD AVFQIQASSE VCKTEIHQFH GTLERVEKLS
     DSTITFDIQL DEGQPDIHFL AGQYVNVGLP NTTETRSYSF SSKPGNRLTS FVVRNVPNGK
     MSEFLSATAQ AGDKMTFAGP FGSFYLRPVT RPVLMLAGGT GIAPFMSMLQ VLEEKGSEHP
     VRLVFGVTND FDLVAIEKLN ELQDKFSWFE YRTVVANPES AHERKGYVTG HIENDWLNNG
     DVDIYLCGPV PMVEAVRGWL DAEGVKPASF LFEKFSAN
//
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