ID E1LBD9_9FIRM Unreviewed; 411 AA.
AC E1LBD9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Metallo-beta-lactamase domain protein {ECO:0000313|EMBL:EFL58143.1};
GN ORFNames=HMPREF9684_1411 {ECO:0000313|EMBL:EFL58143.1};
OS Veillonella atypica ACS-134-V-Col7a.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=866778 {ECO:0000313|EMBL:EFL58143.1, ECO:0000313|Proteomes:UP000005942};
RN [1] {ECO:0000313|EMBL:EFL58143.1, ECO:0000313|Proteomes:UP000005942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-134-V-Col7a {ECO:0000313|EMBL:EFL58143.1,
RC ECO:0000313|Proteomes:UP000005942};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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:EFL58143.1}.
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; AEDS01000036; EFL58143.1; -; Genomic_DNA.
DR RefSeq; WP_005377697.1; NZ_AEDS01000036.1.
DR AlphaFoldDB; E1LBD9; -.
DR Proteomes; UP000005942; 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; PTHR43717; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR PANTHER; PTHR43717:SF1; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 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;
FT DOMAIN 258..399
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 411 AA; 47307 MW; A752ED25C6F06B93 CRC64;
MHCAQKMTHN IYWIGSNDWT TERFENLFPI PNGVSYNSYF IDDEKTCVVD SVDAEIREEY
FDNLSHLLNG RDLDYIIVNH MEPDHCQTLL ETLERYPNCK MVGNATTFRM FEQFYRTPKP
DQYYTVKEGD EICLGKHTLV SYTMPMVHWP EVTCTYEKST GTLFSADAFG TFGTINGNIF
ADQTDFVATY EDEARRYYTN IVGKYGPQVQ NAIRKVSGLE IKRIAPLHGP IWRTPETVEY
ILHKYLHWSS YTAEKKGVVI AFGSMYGNTR DIAQQLAKQL SKRGVTDIKI YDVSKTNASY
IIADAWKYTN LVTIAPTYNL NLYLTMENFI HELKALNFQN HKVSIIGNHS WASAAMKTMV
AHFENDFKDI EIVSQPLDIK SSLKEEDIPL IEKMADDIKA SIDAQEIKEV L
//