ID D7N8U6_9FIRM Unreviewed; 412 AA.
AC D7N8U6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Metallo-beta-lactamase domain protein {ECO:0000313|EMBL:EFI41311.1};
GN ORFNames=HMPREF0629_01369 {ECO:0000313|EMBL:EFI41311.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI41311.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI41311.1, ECO:0000313|Proteomes:UP000004712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI41311.1,
RC ECO:0000313|Proteomes:UP000004712};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-2010) 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}.
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DR EMBL; GL349423; EFI41311.1; -; Genomic_DNA.
DR RefSeq; WP_009222641.1; NZ_GL349423.1.
DR AlphaFoldDB; D7N8U6; -.
DR STRING; 575609.HMPREF0629_01369; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_1_0_9; -.
DR Proteomes; UP000004712; 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; 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; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004712}.
FT DOMAIN 256..397
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 412 AA; 47066 MW; 2E9003309C5A6D75 CRC64;
MHTIRKVVDD LYWVGGNDHR LELFENIFPI PKGVSYNSYL LLDEKTVLVD SVDWSITREY
LRNVEYVLDG RDLDYLLIHH MEPDHCGAIE EICLRYPNVK IISSAQGFDI MRQIGYRIKD
EQIVIVKEGD TMNFGKHTLA FVEAPMVHWP EVILSFDVTN GVLFSADAFG SFGAIDGKLF
NDEVNFDRDW LDEARRYYTN IVGKYGPFVQ DVLKKAATLD IKYICPLHGL VWRSDFGYLL
EKYDKWSKYE PEETGVMIAY ASMYGNTEYA AQALATELCE KGMTNVVIHD VSNTHVSELI
SDTFKYSHIV LASVTYNLGI YPVMKNFIHD MEALNVQNRT VGIIENGTWA CTVGDKMEEF
LNDNLKLIDV LNDRVTINTS LNVANESDMH SLADSIIESM EKIKEIKALA NK
//
