ID A4AFL7_9ACTN Unreviewed; 551 AA.
AC A4AFL7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Putative oxidase {ECO:0000313|EMBL:EAR25773.1};
GN ORFNames=A20C1_07833 {ECO:0000313|EMBL:EAR25773.1};
OS marine actinobacterium PHSC20C1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25773.1, ECO:0000313|Proteomes:UP000003868};
RN [1] {ECO:0000313|EMBL:EAR25773.1, ECO:0000313|Proteomes:UP000003868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25773.1,
RC ECO:0000313|Proteomes:UP000003868};
RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR25773.1}.
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DR EMBL; AAOB01000002; EAR25773.1; -; Genomic_DNA.
DR AlphaFoldDB; A4AFL7; -.
DR STRING; 312284.A20C1_07833; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_11; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000003868; 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:UP000003868}.
FT DOMAIN 469..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 551 AA; 57640 MW; B3971C33441E70FB CRC64;
MSTATTKRTR RILVIGGVAA GMSFATRMRR RDEHAEIVIF ERSGHVSFAN CGLAYYLGGV
ITERDALLLQ TPASLGSRFG LDVRVNHEVA GIDPAGNTIT VHNSLENTTS TEHFDELVIA
TGASATLPAI AGSERMLVLR NIEDVDALHA SLSALDSSTA NVVVLGAGYI GIEMAENLAK
RGLNVTLVQR PAHVLSTLDA EMVTPIEAHL RENGVDLRLG TEAVSIDDST VQLSDGSSVA
ADVVVAAVGV RPDNALAVHA GLAIGTAGGI RVNAGYQTSS PNVYAVGDVA EKVGAVSGEH
ELVALAGPAN RDGRYLADTL AGDDVHSKPA LGTAIVGVFD LTVASLGSTE RTLRATGRDI
RVIHTHPVSH AGYYPGAQSL SLKLIVDADT DLILGAQAVG RDGVDKRMDV LATAASAGLT
ASSLADLELA YAPQYGSAKD PINHLGYVAK NLRDDLSASI QWHEIDAELA AGSLLVDVRT
AAEFGRGAIP QAVNIPLDDL RSRLDEIGDR RVIVHCQVGQ RGHTAVRILS QHGFNVANLD
GGYRTWAAAT A
//
