ID Q8XMA9_CLOPE Unreviewed; 406 AA.
AC Q8XMA9;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Probable flavoprotein {ECO:0000313|EMBL:BAB80487.1};
GN OrderedLocusNames=CPE0781 {ECO:0000313|EMBL:BAB80487.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB80487.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB80487.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB80487.1; -; Genomic_DNA.
DR RefSeq; WP_003455843.1; NC_003366.1.
DR AlphaFoldDB; Q8XMA9; -.
DR STRING; 195102.gene:10490043; -.
DR KEGG; cpe:CPE0781; -.
DR HOGENOM; CLU_017490_0_0_9; -.
DR Proteomes; UP000000818; Chromosome.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000000818}.
FT DOMAIN 251..406
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 406 AA; 46396 MW; 7296C74AE8995628 CRC64;
MNKEIKLRND IYSVGVIDNR PVPFHRLILE KGTTYNSYLL KTRKPTVIDT VDLIYTKDFL
NNLKEIIDLK DISYIVINHT EPDHSGALGG LARQAINAKI VCSEKAVYHL KELYKLHDRD
FIVVNDGDTL DIGGKTLLFK MTPYLHTEET MITYDVEDKI LFPCDIFSTH LTAKEHFSSK
SNEDITEDFL TYYKLIMEPH RKYIRPLIDI LKDLDIEVIA PSHGYILDEN IQSYIDIYDK
YSKETKKGKK ATIVYTTMRN ATKKIAEKFK SELENEDIEV YIFNADKSTK EDILASIKES
DSILFGTSTK YGDLIGSIED ILKELPKLDL SNKLLGAFGS FGWSGEPIEI IQDYLNSTNG
NVLNTSSIIK STGMIDVHFP VRIRFSLNEE SEKEVVRAAD YISSII
//
