ID A1K6J0_AZOSB Unreviewed; 395 AA.
AC A1K6J0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Hypothetical secreted protein {ECO:0000313|EMBL:CAL94445.1};
GN OrderedLocusNames=azo1828 {ECO:0000313|EMBL:CAL94445.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL94445.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL94445.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL94445.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AM406670; CAL94445.1; -; Genomic_DNA.
DR AlphaFoldDB; A1K6J0; -.
DR STRING; 62928.azo1828; -.
DR KEGG; azo:azo1828; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_4; -.
DR Proteomes; UP000002588; Chromosome.
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 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; PR00409; PHDIOXRDTASE.
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:UP000002588}.
FT DOMAIN 67..173
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 314..395
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 42429 MW; 5DD27067F6C0DF87 CRC64;
MARRAPQASV TGQPRRGPFA RSRRRAGMKA VALALAALGL AGLAFIAFLL VDGLRAVYQR
RREERRQRPL RLVVRSREEV GGELLRLTLA HPRRRPLPVF EAGQHLMMTA PAGRGGGAIR
RAYSLAAWHP RPTWYELGIK REAQGAMSSW AWNALLPGAV VDVSPPRGDF VVADDELDLV
LIAGGIGITP MRAMLHASLA RPRARRIVLL HAARHAGTLL YRGEFESLAS LNPHFSYLPI
VSRPDGFWRG ERGRLDAHRV LAAVPTPQQA RFYLCAGQAL MEDLGGGLIA AGIDPARIHS
EAFGAASAGG GHGQVITLED GRRVDTAGEP SLLATLEAHG CAPPSDCRAG SCGECRMRLD
AGAVRWLMAP ACAVADGEIL PCICQPAGDL RLRAA
//
