ID U4T7D6_9GAMM Unreviewed; 722 AA.
AC U4T7D6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:ERL54408.1};
GN ORFNames=M917_2556 {ECO:0000313|EMBL:ERL54408.1};
OS Psychrobacter aquaticus CMS 56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1354303 {ECO:0000313|EMBL:ERL54408.1, ECO:0000313|Proteomes:UP000016761};
RN [1] {ECO:0000313|EMBL:ERL54408.1, ECO:0000313|Proteomes:UP000016761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 56 {ECO:0000313|EMBL:ERL54408.1,
RC ECO:0000313|Proteomes:UP000016761};
RX PubMed=24201199;
RA Reddy G.S., Ara S., Singh A., Kumar Pinnaka A., Shivaji S.;
RT "Draft Genome Sequence of Psychrobacter aquaticus Strain CMS 56T, Isolated
RT from a Cyanobacterial Mat Sample Collected from Water Bodies in the McMurdo
RT Dry Valley Region of Antarctica.";
RL Genome Announc. 1:e00918-13(2013).
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:ERL54408.1}.
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DR EMBL; AUSW01000035; ERL54408.1; -; Genomic_DNA.
DR RefSeq; WP_021815168.1; NZ_AUSW01000035.1.
DR AlphaFoldDB; U4T7D6; -.
DR STRING; 1354303.M917_2556; -.
DR PATRIC; fig|1354303.4.peg.2514; -.
DR eggNOG; COG0398; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000016761; 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..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..183
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 238..566
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 588..694
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 722 AA; 80243 MW; 5F9D3F01FE6564C0 CRC64;
MIKKIALVLV VSMLIISFFY FDLNELLTLD GLKSSMGQFD QYKAQSPWLV IGGFFFVYIL
VTALSLPGAT IMTLAAGALF GLFQGLLIAS FASSIGATLA FLVSRYLLRD SIKQRFPERL
LSIDSGIKKE GAFYLFTLRL VPIFPFFLIN LLMGVTAIKV KTFYWVSQIG MLAGTLVYVN
AGTQLAQIES LSNIFSFNLL ASFALLGLFP LFAKGILNIL KKRRVYKSYT KPKTFDRNMI
VIGAGAGGLV TSYIAATVKA KVTLIEAGEM GGDCLNYGCV PSKALIKSAK VVEQMRNGER
YGLNNSQPEF SFKNVMSRIH EVIADIAPND SVERYSNLGV EVLKGYAKFV DPWTIEIALN
DGRTQRLTAR SIVIATGAHP FVPNLPGLEE TGYVTSDTLW NTFSKLEKPP NKLVVLGGGP
IGSELAQAFA RLGSNVKQIE RGERLLKKED AEVSEFAQQV LIESGVDVLT SHQAIRCETR
DDKKYLIVER YSESTDKQEM AIEYDELICA VGRSARLEGY GLESLGIETE RTINTDEYLE
TLYPNIYAAG DIVGPYQFTH MAAHQAWYAA VNGLFGNLKK FKVDYRVVPW TTFLDPEIAR
VGLNEQEAID KGIDFEITRY DFKDLDRAVT ESANHGFIKV ITPKGKDKIL GVTIVAEHAG
DLMAEFILAM KHGLGLNKIL GTIHIYPTWT EGNKYAAGEW KRNHAPEKIL NLLEKYHTWR
RG
//
