ID B4VKQ9_9CYAN Unreviewed; 514 AA.
AC B4VKQ9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme GidA, putative {ECO:0000313|EMBL:EDX77319.1};
GN ORFNames=MC7420_456 {ECO:0000313|EMBL:EDX77319.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX77319.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX77319.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX77319.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; DS989844; EDX77319.1; -; Genomic_DNA.
DR RefSeq; WP_006099431.1; NZ_DS989844.1.
DR AlphaFoldDB; B4VKQ9; -.
DR STRING; 118168.MC7420_456; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_3; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT DOMAIN 38..356
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 382..491
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 213..220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 77..82
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 514 AA; 56351 MW; 370D06C737A9F52F CRC64;
MTSTSERVIV PPMDDYNQQL VSHVHPPDWV NPKPADRYDL VVIGAGTAGL VTAAGAAGMD
IGLKVALIER HLMGGDCLNV GCVPSKCIIR SSRVVAQMKE AGDFGIRPPE QIDIDFSAVM
ERMRKLRAGI SHHDSAQRFK QTYNIDIFLG EGSFQDSNTI AVGDKILRFK KAVITTGARA
VRPSIEGIEE TGFLTNETVF SLTERPKRLA VIGGGPIGCE LAQAFRRLGC EVILFHRHSH
LLNKEDTDAA EIVQHKFEQE GIRLVLDCKM KRAVKMDEGK LLHYTCNGQD ESIIVDEILV
GAGRAPNIEG LNLDAVGVEY HRKGIKVNDY LQTTNRNIYA AGDICMKWKF THAADAAARI
VIKNTLFSPF GLGRSKLSDL VMPWVTYTDP EIAHVGMYED EAQEKGMKVS TIKIPFNTVD
RAIADGEEDG FVKIHHQKGS DKILGATIVA RHAGEMISEV TTAIVGNVGL SKLSSAIHPY
PTQAEGIKKA ADAYRRTLLT PNTKRFLGLL TKLS
//
