ID D0I9B9_GRIHO Unreviewed; 548 AA.
AC D0I9B9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative NADH oxidase {ECO:0000313|EMBL:EEY72034.1};
GN ORFNames=VHA_002456 {ECO:0000313|EMBL:EEY72034.1};
OS Grimontia hollisae CIP 101886.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY72034.1, ECO:0000313|Proteomes:UP000003604};
RN [1] {ECO:0000313|EMBL:EEY72034.1, ECO:0000313|Proteomes:UP000003604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY72034.1,
RC ECO:0000313|Proteomes:UP000003604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EEY72034.1}.
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DR EMBL; ADAQ01000012; EEY72034.1; -; Genomic_DNA.
DR RefSeq; WP_005504893.1; NZ_ADAQ01000012.1.
DR AlphaFoldDB; D0I9B9; -.
DR GeneID; 58894847; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000003604; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01524; RHOD_Pyr_redox; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003604}.
FT DOMAIN 464..548
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 548 AA; 59483 MW; 2757063B27715D06 CRC64;
MVKILIVGGV AGGASAAARA RRLSEDAEII MFERGEFVSF ANCGLPYHIG GDIKDRAKLL
LQTPESFLAR FNVDVRVMNE VISINRDTKT VTVKNLLEGT EYEERYDFLL LSPGASPVVP
PITGIDNPLT FSLRNIPDMD RIINAIQSNK PTHATVVGGG FIGLEMMEAF HQLGIQTSLV
EMADQVMTPV DKEMAGFVHQ EIRAKGIDLR LGTALESVEH HGNGLTLSFS SGEQLETGLL
IMAIGVRPEI SLAKAAGLKI GELGGIWVNE EMQTSDPFIY AVGDAVEEKD LVTGKQTLVP
LAGPANRQGR MAADNMLGAR ETYQGTQGTA ICKVFDLAVA STGKNEKTLQ REGIGYEKVY
VHTASHASYY PGAEVVSLKL LFAPDSGKIL GAQAVGKDGV DKRIDILAVA QRAGMTVEQL
QHVELTYAPP YGSAKDVINQ AAFVATNVMK GDVRAIHYHD IESLTDDQIL LDVRNPGELE
SVGCFPNALN IPVDQLRQRI NELPKEKEIV VACQVGLRGN VAYRQLVNNG FKARNLLGGY
RTWKFAQQ
//
