ID N2B7S9_9FIRM Unreviewed; 856 AA.
AC N2B7S9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMZ36451.1};
GN ORFNames=C823_00819 {ECO:0000313|EMBL:EMZ36451.1};
OS Eubacterium plexicaudatum ASF492.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ36451.1, ECO:0000313|Proteomes:UP000012589};
RN [1] {ECO:0000313|EMBL:EMZ36451.1, ECO:0000313|Proteomes:UP000012589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF492 {ECO:0000313|EMBL:EMZ36451.1,
RC ECO:0000313|Proteomes:UP000012589};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:EMZ36451.1}.
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DR EMBL; AQFT01000023; EMZ36451.1; -; Genomic_DNA.
DR RefSeq; WP_004053609.1; NZ_AQFT02000001.1.
DR AlphaFoldDB; N2B7S9; -.
DR STRING; 1235802.C823_00819; -.
DR GeneID; 78432391; -.
DR PATRIC; fig|1235802.3.peg.878; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR eggNOG; COG2221; Bacteria.
DR HOGENOM; CLU_333644_0_0_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000012589; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000012589}.
FT DOMAIN 463..533
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 708..738
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 739..769
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 856 AA; 91454 MW; 8B69A1A451C3236D CRC64;
MKYVIVGGVA AGTKAAAKLK RCDRSADVKI FTKGQDISYA GCGLPYYIGG DIPSRENLIV
NTPAKYAGLT GAEILTGCEA VKLDGGNKTV HFKKVTGEAF TETYDRLIIA TGAEPFVPPV
DGVDLAGVFC VRTPDDAVSA RTYIEENSCK KAVVCGAGFI GLEVAENLMA QGLEVTVIDA
APQIMPNAFD AEMADYAKKQ LKAAGMRVRT STALTAIAGT QKAEKVITGQ GTIAADLVIL
AIGVRPATGF LADSGLEMFK GTILTDARMK TNLEDIYAVG DCAMVKNAQT GQAQWSAMGS
TANIAARAMA KSMHGLGNGY GGCLGTGVVR LLPRFNGGRT GLTEAQAQAA GYKTTSIVCV
VDDKAHYYPD ASTFVVKLIA ETASRKLLGI QVFGAGAVDK MTDIAVTGIA QAMKVDDFDT
LDFAYAPPFS TAIHPFVTAC YILENKLDGI FTSMSPAEYA DGAAKGYTVL DVQPAPALAN
ARFVDLASVN GPLEGLDKDA KLLLVCARGK RGYFLQNRLK ACGYTNTKVL EGGAFFNEVK
VPRDKARLSP EEIKRVKGLG CLQDKRYDDV FNVRVITRNG KLTAEEQIKV AEAAEKFGSG
EVTMTTRLTL EIQGVSYDNL DALFTFLKEA GLETGGTGSK VRPVVSCKGT TCQYGLIDTF
ALSQKLHDLY YTGYHEVSLP HKFKIAVGGC PNNCVKPDLN DLGIIGQRVP EIDPDKCKGC
TVCQVRNNCP IKAAVLENGK IRIDADGCNH CGRCIGTCPF DAVNELTAGY KVYVGGRWGK
KVAEGRALDR IFTSEEEVVD VVERAILFFR DEGISGERFA DTIARLGFDY VQDKLLNSKI
DKRQILEKTV VGGATC
//
