ID A9M6C8_BRUC2 Unreviewed; 372 AA.
AC A9M6C8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Ferredoxin, leaf L-A {ECO:0000313|EMBL:ABX62524.1};
GN OrderedLocusNames=BCAN_A1497 {ECO:0000313|EMBL:ABX62524.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX62524.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX62524.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) 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; CP000872; ABX62524.1; -; Genomic_DNA.
DR RefSeq; WP_004691000.1; NC_010103.1.
DR AlphaFoldDB; A9M6C8; -.
DR GeneID; 55591112; -.
DR KEGG; bcs:BCAN_A1497; -.
DR HOGENOM; CLU_003827_14_3_5; -.
DR PhylomeDB; A9M6C8; -.
DR Proteomes; UP000001385; Chromosome I.
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; 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; 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 10..122
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 288..372
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 372 AA; 41032 MW; FF64F61EFA80F01B CRC64;
MQPLKYLDEM LPWNDRLQML ECISAIEEAP DVMTFSFKTT EDNWFRYTPG QFVTLELPLE
RADGLGPVLR TYTLSSTPSR PYHISVTVKA RIGSIGTRWM LDNLRPPMKI KAYGPNGDFS
LANHPGDKYL FISAGSGITP MMSMTRWLFD CAPATDVSFI NCARTPDDII FRKELELLSG
RMEAMRLAFI VEQSSARHVW PGLHGRIDRA RLELLAPDFL QREIFCCGPE PFMNGVRGLL
EQAGFNMANY HQESFQPASE ISAVPVPSPL PETGNAAAPS MPPAVAAASV VFSQSGVEVE
CTENDTILLA ARNGGLKIPS ACEFGICGTC KVKCLSGETE MNHNGGIRDD EIAEGYILAC
CNRPRGRVEI DA
//
