ID A8UH73_9FLAO Unreviewed; 539 AA.
AC A8UH73;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 53.
DE RecName: Full=Vitamin K epoxide reductase domain-containing protein {ECO:0000259|SMART:SM00756};
GN ORFNames=FBALC1_13762 {ECO:0000313|EMBL:EDP72172.1};
OS Flavobacteriales bacterium ALC-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72172.1, ECO:0000313|Proteomes:UP000003630};
RN [1] {ECO:0000313|EMBL:EDP72172.1, ECO:0000313|Proteomes:UP000003630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72172.1,
RC ECO:0000313|Proteomes:UP000003630};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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:EDP72172.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABHI01000001; EDP72172.1; -; Genomic_DNA.
DR AlphaFoldDB; A8UH73; -.
DR STRING; 391603.FBALC1_13762; -.
DR eggNOG; COG1651; Bacteria.
DR OrthoDB; 1100563at2; -.
DR Proteomes; UP000003630; Unassembled WGS sequence.
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; cd12921; VKOR_4; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.1440.130; VKOR domain; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR Pfam; PF07884; VKOR; 1.
DR SMART; SM00756; VKc; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 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:UP000003630};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..296
FT /note="Vitamin K epoxide reductase"
FT /evidence="ECO:0000259|SMART:SM00756"
SQ SEQUENCE 539 AA; 61361 MW; A7F1EB1ADE7489EC CRC64;
MKDSLGYLVM RLLHSNKIFI DKKELQFQIE SHPSYPSLHA ITGVFDHFNI DNLALDIPKN
EETLAQLPKT FLAQIETNEG KEFVVALNKG INYQLISSSK NRNTVSIKEF LKQFTGIIVV
VEKTQYIDES KNSSQIYNQI LITLTSVILL SLIFITKPNF ISSLFFITSI LGLVISFAMK
KQEQGQQTVL GNAFCSGESE RKDCNAVLSS NGAALLGNYK LSDLSIIYFL GLSLTIFSLT
LLQHTLTTSF IISFLAVPIT IYSIYYQAIV IKKWCSLCLS IVGVLWVQAT LSIIQFNILN
LSSILWTPLA VSLSSFLLTL TTYNLVLPKL TELSDLNKIK IDFFKFKRNF KVFSTLLEKT
KYHNTIIQND ISEIVLGNPE SKLKIIIITN PFCGYCKPLH TIIEDILRKY SNIVNITIRI
ASKTEDKENE LLKIATHLLG LYHKKGQELC LKAMHDIYNN LAPEKWLEKW EFSHINGDYL
NIIKMQSNWC IDNNLNFTPE ILINGKSFPK EYDRSDLVLF IEDLHESCSI NTTNLQLTT
//
