ID A0A343JFG4_9CLOT Unreviewed; 880 AA.
AC A0A343JFG4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:ASW44272.1};
GN ORFNames=BEN51_12645 {ECO:0000313|EMBL:ASW44272.1};
OS Clostridium isatidis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=182773 {ECO:0000313|EMBL:ASW44272.1, ECO:0000313|Proteomes:UP000264883};
RN [1] {ECO:0000313|EMBL:ASW44272.1, ECO:0000313|Proteomes:UP000264883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15098 {ECO:0000313|EMBL:ASW44272.1,
RC ECO:0000313|Proteomes:UP000264883};
RA Little G.T., Minton N.P.;
RT "Complete Genome Sequence Of The Indigo Reducing Clostridium isatidis
RT DSM15098.";
RL Submitted (AUG-2016) 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}.
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DR EMBL; CP016786; ASW44272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A343JFG4; -.
DR KEGG; cia:BEN51_12645; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000264883; 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:ASW44272.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000264883}.
FT DOMAIN 257..396
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 428..462
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 880 AA; 98269 MW; 36B519FBFD3287C2 CRC64;
MKHLELKKDI YWIGALDPNL RVFDIIMYTP YGTSYNSYVV KGSEKIALFE TVKVQFFDQY
LERLKSLNID ITKIDYIIVD HTEPDHAGSV AKLLELSPNA KIVGSATALS FLKDIANRDF
EAITVKHGSE ISLGNKTLRF ISAPFLHWPD SIYTYIVEDE VLITCDSFGS HYSSENIINS
KVENREHYME ALKYYFDMIF GPFKPYVLKA IDKIKDLKID MILPGHGPVL VENPMEIIEL
YKEWSTPKEA KNKNKVVSIS YVSAYGYTEI LAKEIAKGIE SVENVEARLF NVIENDINNI
VESIEESEGI LFGSPTIVSE LLPPVRDVLT KLNPVIHGGK LAAAFGSYGW SGEAIPRIET
RLNELNMKLF GPSLKVKFKP SDEELNEAFE FGVRFAETLI GEREFVPFDK EEDTRKKSAD
DTPSGGKLKL WKCIVCGEIF EAETVPDVCP VCGAGSDQFI EIPREENKFT SDTKETIVII
GNGAAGFYAA KAIRERNINA VIKLISNEPE HSYVRTQLSD LITEEPDNTF YLEKENWYKE
NNIIEILGVN VNSIDKDKKI IVLDNNEQIK YDKLILANGS YNFVPPTKVK YETSEIEINS
ENYKTLKGIH TIKKLADVKI IKNELPNVKN VVVVGGGLLG LEAAWELQKK NVKVTVIELA
DRLLPRQLDT EGSNLFKNII TNTPVEILLG EAVDFINADN NGVKSIQLKS GKLIKTDMII
YSVGVRSNIN LAKSTGIECN RGIIVDENMR TNLPDIYACG DVAELNGIYY GNWPAAIEMG
KVAGANAVGD DLKFEKFVSS TIFAAMEANI FSAGSINFDD AALEKIGSIN PEENKYIKLF
FSNNKLVGGI LIDDLSSSVK IIEGIKNGTD KATMLAQNIF
//
