ID   A0A497XJN2_9PROT        Unreviewed;      1255 AA.
AC   A0A497XJN2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:RLJ68162.1};
GN   ORFNames=DFR35_0716 {ECO:0000313|EMBL:RLJ68162.1};
OS   Sulfurisoma sediminicola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Sulfurisoma.
OX   NCBI_TaxID=1381557 {ECO:0000313|EMBL:RLJ68162.1, ECO:0000313|Proteomes:UP000268908};
RN   [1] {ECO:0000313|EMBL:RLJ68162.1, ECO:0000313|Proteomes:UP000268908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26916 {ECO:0000313|EMBL:RLJ68162.1,
RC   ECO:0000313|Proteomes:UP000268908};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-2018) 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:RLJ68162.1}.
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DR   EMBL; RCCI01000004; RLJ68162.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A497XJN2; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000268908; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR021817; DUF3400.
DR   InterPro; IPR022153; DUF3683.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF11880; DUF3400; 1.
DR   Pfam; PF12447; DUF3683; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 2.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268908}.
FT   DOMAIN          159..392
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1255 AA;  138217 MW;  0002D427EA3284F0 CRC64;
     MNARLREIPY NYTSFSDREI VIRLLGAEMW AILDVLRSQR VTGRSARMLY EVLGDIWVVR
     RNPYLEDDLL ANPSRRAALV GALRHRLAEI EKRRQGNEPV AKLLVAAHAA VHSFERWFGD
     TYDLRRRVLR VLAKHTRKDN ICFDGLARVS HVTDATDWRV EYPFVVLTPD TEEEIAPLVR
     GCIELGLTII PRGGGTGYTG GAVPLEAKSA VINTEKLIDM GAVEQAVLPG LDQPYATIRT
     GAGLVTRRVM DRADESGLVF ACDPTSADAS CIGGNIAMNA GGKKAVLWGT ALDNLASWRM
     VTPEGKWLEV ERLNHNLGKI HDQAVATFRC RYFDENGKKL EREETLEIPG AGFRKVGLGK
     DVTDKFLAGL PGVQKEGCDG LITSAVWILH KMPPVARTVC LEFFGQVRDA VPSIVEITEY
     LKARPGGAIL AGLEHLDERY VKAVGYATKA KRHGRPKMVL IGDIVGADED AVMRATSEVV
     KIANSRGGEG FIAVSADARK KFWLDRARTA AISRHTNAFK VNEDVVIPLP RMGDYCDGID
     RINIELSIAN KLALCDALAE CLAGDLPLHA GDTELDKNEL LGDRREQALE LIAATRSKWQ
     ALLDDIGHNF NALQEHSIRV SWKTELKAPL EAIFDGNAFR PVVERIEGIH KEVLRGRVFV
     ALHMHAGDGN VHTNIPVNSD NYAMLQTASK AVARIMALAR SLGGVISGEH GIGITKLEFL
     TDDEIRPFRD YKRRVDPDGR FNKGKLMAGA DLANAYTPSF SLLGTESLIM EQSEIGSISA
     SIKDCLRCGK CKPVCSTHVP RANLLYSPRN KILGTSLLIE AFLYEEQTRR GISLQHFDEF
     NDVADHCTVC HKCVNPCPVD IDFGDVSIAM RNFLRAQGKK KTSPGAIAAM AFLNATDPAT
     IKLLRTGMIE WGYKAQRLGH RLAKSFGLIQ ETVQRPPATL GRPAIKAQVI HFLNKPMPAS
     LPSRTSRALL DIEDDAQIPV IRDPKKSTEE SDAVFYFPGC GSERLFSQVG LATQAMLYDL
     GATTVLPPGY LCCGYPQTSN GDEDKGQAIT TANRVLFHRV ANTLNYLDIK TVIVSCGTCM
     DQLLKYEFDK IFPGCRLLDI HEYLLEKGVK LEGTSGVQFM YHEPCHTPMK THSGIKVVNQ
     LMGQRVDLND RCCGESGTLA VTRPDVSTQI RYRKQQEIEA GAAKLRMIGA GGTADQVKIL
     TSCPSCLQGL ARYRDDANIE ADYVVVEMAK RLLGAEWMED YVAAANAGGI ERVLL
//