VKOR_SYNJB
ID VKOR_SYNJB Reviewed; 283 AA.
AC Q2JJF6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Vitamin K epoxide reductase homolog;
DE Short=VKOR;
DE EC=1.17.4.-;
GN OrderedLocusNames=CYB_2278;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF MUTANT SER-56 IN COMPLEX WITH
RP UBIQUINONE, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND, FUNCTION,
RP MUTAGENESIS OF CYS-50; CYS-56; CYS-130; CYS-133; CYS-209 AND CYS-212,
RP ACTIVITY REGULATION, REDOX-ACTIVE SITE, AND REGION.
RX PubMed=20110994; DOI=10.1038/nature08720;
RA Li W., Schulman S., Dutton R.J., Boyd D., Beckwith J., Rapoport T.A.;
RT "Structure of a bacterial homologue of vitamin K epoxide reductase.";
RL Nature 463:507-512(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 186-283 OF MUTANTS ALA-50 AND
RP ALA-212 IN COMPLEX WITH UBIQUINONE, FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, MUTAGENESIS OF LYS-41; CYS-50; LEU-60; CYS-130 AND CYS-212,
RP REDOX-ACTIVE SITE, SITE, AND THIOREDOXIN-LIKE REGION.
RX PubMed=24477003; DOI=10.1038/ncomms4110;
RA Liu S., Cheng W., Fowle Grider R., Shen G., Li W.;
RT "Structures of an intramembrane vitamin K epoxide reductase homolog reveal
RT control mechanisms for electron transfer.";
RL Nat. Commun. 5:3110-3110(2014).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that catalyzes vitamin K-
CC dependent disulfide bond formation in periplasmic target proteins.
CC {ECO:0000269|PubMed:20110994, ECO:0000269|PubMed:24477003}.
CC -!- ACTIVITY REGULATION: Inhibited by ferulenol.
CC {ECO:0000269|PubMed:20110994}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20110994,
CC ECO:0000269|PubMed:24477003}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20110994, ECO:0000269|PubMed:24477003}.
CC -!- DOMAIN: Cysteine residues from the thioredoxin-like domain participate
CC in a series of disulfide-exchange reactions that regenerate the redox-
CC active cysteine residues in the transmembrane domain.
CC -!- SIMILARITY: Belongs to the VKOR family. {ECO:0000305}.
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DR EMBL; CP000240; ABD03218.1; -; Genomic_DNA.
DR RefSeq; WP_011433847.1; NC_007776.1.
DR PDB; 3KP8; X-ray; 1.66 A; A=186-283.
DR PDB; 3KP9; X-ray; 3.60 A; A=1-283.
DR PDB; 4NV2; X-ray; 3.61 A; A=1-283.
DR PDB; 4NV5; X-ray; 2.79 A; A/B=1-283.
DR PDB; 4NV6; X-ray; 4.19 A; A=1-283.
DR PDBsum; 3KP8; -.
DR PDBsum; 3KP9; -.
DR PDBsum; 4NV2; -.
DR PDBsum; 4NV5; -.
DR PDBsum; 4NV6; -.
DR AlphaFoldDB; Q2JJF6; -.
DR SMR; Q2JJF6; -.
DR STRING; 321332.CYB_2278; -.
DR KEGG; cyb:CYB_2278; -.
DR eggNOG; COG4243; Bacteria.
DR HOGENOM; CLU_047345_0_0_3; -.
DR OMA; WCPHCHE; -.
DR OrthoDB; 1187526at2; -.
DR BRENDA; 1.17.4.4; 15616.
DR EvolutionaryTrace; Q2JJF6; -.
DR Proteomes; UP000001938; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd12916; VKOR_1; 1.
DR Gene3D; 1.20.1440.130; -; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR044698; VKOR/LTO1.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF07884; VKOR; 1.
DR SMART; SM00756; VKc; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Membrane; Oxidoreductase; Quinone;
KW Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Vitamin K epoxide reductase homolog"
FT /id="PRO_0000429265"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT TRANSMEM 21..41
FT /note="Helical"
FT TOPO_DOM 42..66
FT /note="Periplasmic"
FT TRANSMEM 67..87
FT /note="Helical"
FT TOPO_DOM 88..102
FT /note="Cytoplasmic"
FT TRANSMEM 103..123
FT /note="Helical"
FT TOPO_DOM 124..128
FT /note="Periplasmic"
FT TRANSMEM 129..149
FT /note="Helical"
FT TOPO_DOM 150..158
FT /note="Cytoplasmic"
FT TRANSMEM 159..179
FT /note="Helical"
FT TOPO_DOM 180..283
FT /note="Periplasmic"
FT REGION 186..283
FT /note="Thioredoxin-like domain"
FT BINDING 59..65
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT BINDING 111..122
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT SITE 50
FT /note="Important for the reduction of the redox-active Cys-
FT 130 and Cys-133"
FT SITE 56
FT /note="Important for the reduction of the redox-active Cys-
FT 130 and Cys-133"
FT SITE 209
FT /note="Important for the reduction of the redox-active Cys-
FT 130 and Cys-133"
FT SITE 212
FT /note="Important for the reduction of the redox-active Cys-
FT 130 and Cys-133"
FT DISULFID 50..56
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:20110994"
FT DISULFID 130..133
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:20110994"
FT DISULFID 209..212
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:20110994"
FT DISULFID 231..244
FT /evidence="ECO:0000269|PubMed:20110994"
FT MUTAGEN 41
FT /note="K->A: Reduces enzyme activity by about 40% with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:24477003"
FT MUTAGEN 41
FT /note="K->E: Reduces enzyme activity by about 20% with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:24477003"
FT MUTAGEN 41
FT /note="K->R: Minor effect on enzyme activity with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:24477003"
FT MUTAGEN 41
FT /note="K->S: Reduces enzyme activity by about 75% with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:24477003"
FT MUTAGEN 50
FT /note="C->A: Abolishes enzyme activity, but not with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:20110994,
FT ECO:0000269|PubMed:24477003"
FT MUTAGEN 56
FT /note="C->A: Abolishes enzyme activity, but not with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:20110994"
FT MUTAGEN 60
FT /note="L->A,G: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:24477003"
FT MUTAGEN 130
FT /note="C->A,S: Abolishes enzyme activity, also with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:20110994,
FT ECO:0000269|PubMed:24477003"
FT MUTAGEN 133
FT /note="C->A: Abolishes enzyme activity, also with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:20110994"
FT MUTAGEN 209
FT /note="C->A: Abolishes enzyme activity, but not with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:20110994"
FT MUTAGEN 212
FT /note="C->A: Abolishes enzyme activity, but not with
FT dithiothreitol as in vitro reductant."
FT /evidence="ECO:0000269|PubMed:20110994,
FT ECO:0000269|PubMed:24477003"
FT HELIX 21..42
FT /evidence="ECO:0007829|PDB:4NV5"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:4NV5"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4NV5"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:4NV5"
FT HELIX 96..124
FT /evidence="ECO:0007829|PDB:4NV5"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:4NV5"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4NV5"
FT HELIX 157..181
FT /evidence="ECO:0007829|PDB:4NV5"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:3KP8"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3KP8"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:3KP8"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3KP8"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3KP8"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:3KP8"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:3KP8"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:3KP8"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:3KP8"
SQ SEQUENCE 283 AA; 30593 MW; 615561731469DF16 CRC64;
MASYLKLKAQ EETWLQRHSR LILAILAGLG SLLTAYLTYT KLTEQPAAFC TGDGGCDLVL
SSRWAEFLGI PTAAVGLLGF LGVLALAVLP DGLPLVKRWR WPALFGLVSA MTAFEMYMLY
LMVAVLRQFC MYCTTAIILV AGLGLVTVLG HRWLDGGKLA FSYILVAFLT LVTTIGVYAN
QVPPPSPLAV GLAAHLRQIG GTMYGAYWCP HCQDQKELFG AAFDQVPYVE CSPNGPGTPQ
AQECTEAGIT SYPTWIINGR TYTGVRSLEA LAVASGYPLE EGR
