ID   A0A1Z9X2M0_9ALTE        Unreviewed;       717 AA.
AC   A0A1Z9X2M0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OUX84211.1};
GN   ORFNames=CBB95_16860 {ECO:0000313|EMBL:OUX84211.1};
OS   Alteromonas sp. TMED35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1986603 {ECO:0000313|EMBL:OUX84211.1, ECO:0000313|Proteomes:UP000196497};
RN   [1] {ECO:0000313|EMBL:OUX84211.1, ECO:0000313|Proteomes:UP000196497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED35 {ECO:0000313|EMBL:OUX84211.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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:OUX84211.1}.
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DR   EMBL; NHCO01000098; OUX84211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9X2M0; -.
DR   Proteomes; UP000196497; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR032816; VTT_dom.
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   Pfam; PF09335; SNARE_assoc; 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|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..183
FT                   /note="VTT"
FT                   /evidence="ECO:0000259|Pfam:PF09335"
FT   DOMAIN          238..561
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          583..691
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   717 AA;  78594 MW;  0DAD2A9315441EFE CRC64;
     MFKKIALLAV IAAAVVGFFY FDLNTYLTLE GMKGSLDTFK TQISENPVLS IAIFFAIYVA
     VTALSLPGAA ILTLAAGALF GLFKGLIIVS FASSLGATLA FLVARFILRD TVRNKFKEKL
     KKIDEGVEKQ GPFYLFTLRL VPVFPFFLIN LLMGLTSIKT WTFYWVSQVG MLAGTVVYVN
     AGTQLAQIDS LSGILSPELL FSFVLLGIFP WIAKGIVAIV NRRRVYKGYS KPKTFDRNLV
     VIGAGAGGLV TSYIAAAVKA KVTLIEAGEM GGDCLNYGCV PSKAIIKTAK VANQMRHADD
     YGLNPVSPSM SFKKVMKRVH EVIATIAPND SVERYTNLGV DVVKGYATII DPWTVEIKTN
     EGDVKRLTTK NIVVATGASP FIPELPGIEE SGYVTSDTLW TKFAELDDAP KRLIVLGGGP
     IGCELAQAFA RLGSEVTQVE RAPRLMGRED TDVADYVQSV LTESNVNVLT QHDALRFETR
     GDDKVLVVAK DGNEIDVAYD EVIIAVGRKA RLNGFGLEKL GIQFDRTIET DEYLQTLMPN
     IYAAGDVVGP YQFTHVAAHQ AWFAAVNALF GTFKKFKVDY SVIPWTTFID PEVARVGLSE
     RDAVERDIDV EVTRYEFAEL DRAVTESARK GFIKVLTPPG KDKILGVTVV SEHAGDLLAE
     FVIAMKHGLG LNKILGTIHT YPTWAEGAKY AAGNWKRANQ PEKLLSFVEK FHTWRRG
//