ID A0A410PQP0_9CLOT Unreviewed; 850 AA.
AC A0A410PQP0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:QAT41277.1};
GN ORFNames=EQM05_13925 {ECO:0000313|EMBL:QAT41277.1};
OS Clostridium sp. JN-9.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2507159 {ECO:0000313|EMBL:QAT41277.1, ECO:0000313|Proteomes:UP000287890};
RN [1] {ECO:0000313|EMBL:QAT41277.1, ECO:0000313|Proteomes:UP000287890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN-9 {ECO:0000313|EMBL:QAT41277.1,
RC ECO:0000313|Proteomes:UP000287890};
RA Ma S.;
RT "Draft genomes of a novel of Clostridium strains.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP035280; QAT41277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410PQP0; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000287890; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR CDD; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR CDD; cd00729; rubredoxin_SM; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR045761; ODP_dom.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR041575; Rubredoxin_C.
DR InterPro; IPR048574; RUBY_RBDX.
DR PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR PANTHER; PTHR32145:SF11; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF19583; ODP; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR Pfam; PF21349; RUBY_RBDX; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:QAT41277.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287890}.
FT DOMAIN 257..396
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 415..449
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 850 AA; 94202 MW; E0576872F1A3E139 CRC64;
MKAMEVKKDI YWIGALDPNL RTFDIVMHTP YGTTYNSYIV KGSEKTAVVE TVKEKFFDQY
IDRLNSLNID PSKIDYIIVD HTEPDHAGSI AKLLDIAKNA VVVGSAAAIK FSKAIANRDF
KSLVVNNGDT LSLGNKTLKF ISAPMLHWPD TIYTYAEEDK LLFTCDSFGA HYCNENVFND
LNPSQKDYNE ALKHYFDCII SPFKPYVLKA IDKIKDLDID MICTGHGPIL RENPWKVVNL
YKEWSLPKQK DNNDGNIVMC YVSAYGYTES IANKIEEGVK SAGNFNFKKY DVEHNEIPDI
IEKINDADGL LFGSPTMLGD ALKPIWEVLY SLNPIIHGGK IAAVFGSYGW SGEAVRNMEE
RLKQLRMNII KPGLRINFKP TEDELKQAYN FGQSFAKKIQ EKLSKGVKPS KPATLKKWKC
LICGEIFEGA EPPKICPVCG ATQDQFIEVQ DSVKTFANDT DEKFVIIGNG AAGYYAAESI
RSRNKKAGIQ FISGESKPCY YRPVLSDYLN SEIEDKDFYV TNKDWYNDNN IKLTLNSFVN
KIDTKNKKVF LNNGAEAEYD KLILANGSSN FIPPIPGNTK EGVFTLKYLS DADKIKAYFT
KVKKAVVIGG GLLGLEAAWE MKKAGLDVTV VEFFDRLLPR QLDKEGAEIF KKIVDNSGVK
IILGSSAVEI LGDSNVTGIK LNNGETLDCE MVLFSVGIRP NKALAEAAGI KCDKGILVND
KMMTNIDSVY ACGDVAQING RVYGNWPAAV GMGKVAGANA CGDESYFNDF VSSVVFSSMN
ADLFSCGSFD EGCEELAVKD ASKGIYKKLF FKNDKLVGAM LIGDTKKSGK ITLAIQSGKT
FNDVLTENLL
//
