ID A0A1R1ICK6_9RHOO Unreviewed; 350 AA.
AC A0A1R1ICK6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:OMG56299.1};
GN ORFNames=BJN45_01345 {ECO:0000313|EMBL:OMG56299.1};
OS Azonexus hydrophilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Azonexus.
OX NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG56299.1, ECO:0000313|Proteomes:UP000187526};
RN [1] {ECO:0000313|EMBL:OMG56299.1, ECO:0000313|Proteomes:UP000187526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS02 {ECO:0000313|EMBL:OMG56299.1,
RC ECO:0000313|Proteomes:UP000187526};
RA Salah Z., Rout S.P., Humphreys P.N.;
RT "Alkaliphiles isolated from bioreactors.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OMG56299.1}.
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DR EMBL; MTHD01000001; OMG56299.1; -; Genomic_DNA.
DR RefSeq; WP_076091315.1; NZ_MTHD01000001.1.
DR AlphaFoldDB; A0A1R1ICK6; -.
DR STRING; 418702.BJN45_01345; -.
DR OrthoDB; 370747at2; -.
DR Proteomes; UP000187526; 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; cd06187; O2ase_reductase_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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000187526}.
FT DOMAIN 2..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 350 AA; 38354 MW; A8788DC53F1BC19D CRC64;
MAKIIMQPSG KSVECAYGDT VLMALEKAGY ALPNNCRAGA CGECKVKVTT GQFDQGMVLD
MALSQEERKQ GYGLMCMAKP ISEEITIEWG TEDAKPKLFP PREDALFVVI DKRQVAARVV
ELRLRPVGLP IRYWPGQYVT LGNARDNIPP RAYSISNAPR PDGELVLQVA RQDGGLTSAW
VHDSLQVGDN VKISGAYGTF IGDPSVDTPV LCLAAGTGLA PILALAEAAL RRGYKRPVGL
VFSARSKEDV YSQGMMAWWR TKHRNFDYKI TLTREEAEGF QSGRIDAVLP KLFPDLSKHS
IFAAGSPEFV ETCVATVKKL GARPELIHTE GFFSQQVQLA GEDDPFKLPF
//
