ID A0A0K2GEL8_NITMO Unreviewed; 469 AA.
AC A0A0K2GEL8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Vitamin K epoxide reductase {ECO:0000313|EMBL:ALA59304.1};
GN ORFNames=NITMOv2_2898 {ECO:0000313|EMBL:ALA59304.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA59304.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA59304.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA59304.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the VKOR family.
CC {ECO:0000256|ARBA:ARBA00006214}.
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DR EMBL; CP011801; ALA59304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2GEL8; -.
DR STRING; 42253.NITMOv2_2898; -.
DR KEGG; nmv:NITMOv2_2898; -.
DR PATRIC; fig|42253.5.peg.2866; -.
DR Proteomes; UP000069205; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd12919; VKOR_2; 1.
DR Gene3D; 1.20.1440.130; VKOR domain; 1.
DR InterPro; IPR005530; SPW.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF03779; SPW; 2.
DR Pfam; PF07884; VKOR; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..298
FT /note="Vitamin K epoxide reductase"
FT /evidence="ECO:0000259|Pfam:PF07884"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 50757 MW; 29366B89E7E91BAE CRC64;
MASRQATHQE HQHSRHPAAM ETTHEGMSVA EHGSMLAENH KKFLWTYHTN LLLGIWLLTS
PVTFGYQSTG MTWSDIASGG LVLAFGTLAL FRRVWAAWAV CFTGIWLLFA PLVFWAPSAT
AYLNDTIVGG MLIALSILIP GMPGMGWMDM PGPEIPPGWT YNPSTWLQRG PIIALAFVGF
FIARYLAAYQ LGHIPSAWDP FFGDSTQQVL TSKVSKAWPI SDAGLGALSY LLEALSGYMG
DSRRWRTMPW MVLMFALLVV PLGATSIILV ILQPVSIGMW CTLCLVAAVA MLIMVPLAVD
EVVAMGQFMV ASSRAGKPFW QTFWKGGSIE GGGPDTRSPE FGSPASAVGP SMIWGVSLPW
TLAVGTALGM WLMVAPSVLG TDAAIADSDH LVGALVVTFA VIAWAEVTRS VRWFNAVLGL
WLIAAPWLLA GGISMATLND LVVGLLLVLT SLPLGTIRER YAGWSRYII
//
