ID R6GRZ9_9CLOT Unreviewed; 415 AA.
AC R6GRZ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Beta-lactamase domain protein {ECO:0000313|EMBL:CDB16947.1};
GN ORFNames=BN542_02125 {ECO:0000313|EMBL:CDB16947.1};
OS Clostridium sp. CAG:221.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB16947.1, ECO:0000313|Proteomes:UP000018176};
RN [1] {ECO:0000313|EMBL:CDB16947.1, ECO:0000313|Proteomes:UP000018176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDB16947.1}.
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DR EMBL; CBDC010000121; CDB16947.1; -; Genomic_DNA.
DR AlphaFoldDB; R6GRZ9; -.
DR Proteomes; UP000018176; 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:SF11; DIFLAVIN FLAVOPROTEIN A 2-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;
FT DOMAIN 258..398
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 415 AA; 46613 MW; 973C75AE67DE5200 CRC64;
MCKTISINPD LTWVGALDPN LRIFDIIMET KFGTTYNSYV LKGTEGVAIF ETVKEKFFDE
HLEKIKSVVK PEDITYIVVN HTEPDHAGSV GKLLEFAPNA TVVGSSLAIR YMGQIMNKPF
KNKIVKDGET ISLGNKTIKF LSVPQLHWPD TMYSYVIEDE TLITCDSFGA HYSDERVIKS
QLEAEKEDDY IEAYNYYFSM IMGPFKPFVL KALDKIKDLS IKFICPGHGM VLDGANIEKY
MELYREWSQP VKRETPSIVI PYVSAYGYTA ELAEKVKEGI ESLEENVDVL MYDLVYADIN
EVIAEINKCS GLLIGSPTLL ADTLPPIWTI LGSLNPVIHR GLHASCFGSY GWSGDALKNI
EQRFNQLKFT IPVAPLGVMF KPSEDELEKA FAFGHDFAKE TLQCVNGGQC NIQAQ
//