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Database: UniProt
Entry: A0A084JD20_9CLOT
LinkDB: A0A084JD20_9CLOT
Original site: A0A084JD20_9CLOT 
ID   A0A084JD20_9CLOT        Unreviewed;       399 AA.
AC   A0A084JD20;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Beta-lactamase {ECO:0000313|EMBL:KEZ86854.1};
GN   ORFNames=IO99_08215 {ECO:0000313|EMBL:KEZ86854.1};
OS   Clostridium sulfidigenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ86854.1, ECO:0000313|Proteomes:UP000028542};
RN   [1] {ECO:0000313|EMBL:KEZ86854.1, ECO:0000313|Proteomes:UP000028542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=113A {ECO:0000313|EMBL:KEZ86854.1,
RC   ECO:0000313|Proteomes:UP000028542};
RA   Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT   "Draft genome of Clostridium sulfidigenes 113A isolated from sediments
RT   associated with methane hydrate from Krishna Godavari basin.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC       hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
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:KEZ86854.1}.
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DR   EMBL; JPMD01000017; KEZ86854.1; -; Genomic_DNA.
DR   RefSeq; WP_035132141.1; NZ_JPMD01000017.1.
DR   AlphaFoldDB; A0A084JD20; -.
DR   STRING; 318464.IO99_08215; -.
DR   GeneID; 84601020; -.
DR   eggNOG; COG0426; Bacteria.
DR   Proteomes; UP000028542; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal 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   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
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; IPR016440; Rubredoxin-O_OxRdtase.
DR   PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR   PANTHER; PTHR32145:SF20; FLAVOPROTEIN-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF19583; ODP; 1.
DR   PIRSF; PIRSF005243; ROO; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028542}.
FT   DOMAIN          255..395
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   399 AA;  45524 MW;  37C825CE03F215F4 CRC64;
     MFCVRKITED LYWVGGNDRR LALFENIHPI PRGVSYNSYL LLDKKTVLFD TVDWSICRQF
     LENIQAVLNG RPLDYLVINH MEPDHGAAIE EIILRYPDVK IISTEKSFLL MRQFGFEIDG
     RMEEVVEGDI KSFGKHEVTF VAAPMVHWPE AMVTFDTTNG VLFSADAFGS FGALDGKLFN
     DEVDFDRDWI DDARRYYTNI VGKYGPHVQE LLKKASGLDI KMICPLHGPV WRTDLGYFID
     KYDKWSRYEP EEKAVMIVYA SMYGNTEAAA TALATKFVEK GMKNVVMYDV SSTHVSELIS
     ETFRVSHVVL ASVTYNLGIY PPMHNYLMDM KALNLQKRTF AIIENGSWAC KSGSLMSEFL
     EEMREMTVLE DKVTLVSSMN EGNVTDMDTI VEGVIESMK
//
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